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Title :   GABACULIEN COMPLEX OF GABACULINE RESISTANT GSAM VERSION

Authors :   J. Stetefeld

Date :   07 Jan 09 (Deposition) - 24 Nov 09 (Release) - 09 Feb 10 (Revision)

Method :   X-RAY DIFFRACTION

Resolution :   2.35

Chains :   Asym./Biol. Unit : A,B

Keywords :   Drug Resistance, Microevilution, Integrated Approach, Chlorophyll Biosynthesis, Cytoplasm, Isomerase, Porphyrin Biosynthesis, Pyridoxal Phosphate (Keyword Search: [Gene Ontology, PubMed, Web (Google)] )

Reference :   G. L. Orriss, T. R. Patel, J. Sorensen, J. Stetefeld
Absence Of A Catalytic Water Confers Resistance To The Neurotoxin Gabaculine.
Faseb J. V. 24 404 2010
PubMed-ID: 19786580 | Reference-DOI: 10.1096/FJ.09-138297

Molecule 1 - GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE
	Chains	:	A, B
	EC Number	:	5.4.3.8
	Engineered	:	YES
	Expression System	:	ESCHERICHIA COLI
	Expression System Plasmid	:	PSAT 1.4
	Expression System Taxid	:	562
	Expression System Variant	:	K74
	Expression System Vector Type	:	PLASMID
	Gene	:	HEML, GSA, SYC0881_C
	Organism Scientific	:	SYNECHOCOCCUS ELONGATUS PCC 6301
	Organism Taxid	:	269084
	Synonym	:	GSA, GLUTAMATE-1-SEMIALDEHYDE AMINOTRANSFERASE, GSA-AT

		1	2
Asymmetric/Biological Unit	:	A	B

Summary Information (see also Sequences/Alignments below)

Asymmetric/Biological Unit (2, 3)

No.	Name	Count	Type	Full Name
1	GAB	1	Ligand/Ion	3-AMINOBENZOIC ACID
2	PMP	2	Ligand/Ion	4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE

Asymmetric Unit (3, 3)

No.	Name	Evidence	Residues	Description
1	AC1	SOFTWARE	GLY A:1123 , THR A:1124 , TYR A:1150 , ASN A:1217 , ASP A:1245 , VAL A:1247 , ILE A:1248 , LYS A:1273 , GAB A:2000 , HOH A:7052 , HOH A:7192 , HOH A:7245 , GLY B:2304 , THR B:2305	BINDING SITE FOR RESIDUE PMP A1434
2	AC2	SOFTWARE	SER A:1029 , ARG A:1032 , TRP A:1067 , TYR A:1150 , PMP A:1434 , HOH A:7245 , ALA B:2303 , GLY B:2304 , THR B:2305	BINDING SITE FOR RESIDUE GAB A2000
3	AC3	SOFTWARE	THR A:1305 , SER B:2122 , GLY B:2123 , THR B:2124 , TYR B:2150 , GLU B:2212 , ASN B:2217 , ASP B:2245 , VAL B:2247 , ILE B:2248 , LYS B:2273 , HOH B:7095 , HOH B:7096 , HOH B:7097 , HOH B:7139	BINDING SITE FOR RESIDUE PMP B2434

(no "SS Bond" information available for 3FQA)

Asymmetric/Biological Unit

No.	Residues
1	Ala A:1295	-	Pro A:1296
2	Gly A:1370	-	Pro A:1371
3	Ser B:2173	-	Pro B:2174
4	Ala B:2295	-	Pro B:2296
5	Gly B:2370	-	Pro B:2371

(no "SAP(SNP)/Variant" information available for 3FQA)

Asymmetric/Biological Unit (1, 2)

	PROSITE			UniProtKB		PDB
No.	ID	AC	Description	ID	Location	Count	Location
1	AA_TRANSFER_CLASS_3	PS00600	Aminotransferases class-III pyridoxal-phosphate attachment site.	GSA_SYNP6	242-278	2	A:1242-1278 B:2242-2278

(no "Exon" information available for 3FQA)

Asymmetric/Biological Unit

Reformat:	Number of residues per line = ('0' or empty: single-line sequence representation)
	Number of residues per labelling interval =
	UniProt sequence: complete aligned part

Show mapping:	SCOP domains	CATH domains	Pfam domains	Secondary structure (by author)
	SAPs(SNPs)	PROSITE motifs	Exons
	(details for a mapped element are shown in a popup box when the mouse pointer rests over it)

Chain A from PDB  Type:PROTEIN  Length:426
 aligned with GSA_SYNP6 | P24630 from UniProtKB/Swiss-Prot  Length:433

    Alignment length:426
                                    17        27        37        47        57        67        77        87        97       107       117       127       137       147       157       167       177       187       197       207       217       227       237       247       257       267       277       287       297       307       317       327       337       347       357       367       377       387       397       407       417       427      
           GSA_SYNP6      8 KTIKSDEIFAAAQKLMPGGVSSPVRAFKSVGGQPIVFDRVKDAYAWDVDGNRYIDYVGTWGPAICGHAHPEVIEALKVAMEKGTSFGAPCALENVLAEMVIDAVPSIEMVRFVNSGTEACMAVLRLMRAYTGRDKIIKFEGCYHGHADMFLVKAGSGVATLGLPDSPGVPKSTTANTLTAPYNDLEAVKALFAENPGEIAGVILEPIVGNSGFIVPDAGFLEGLREITLEHDALLVFDEVMTGFRIAYGGVQEKFGVTPDLTTLGKIIGGGLPVGAYGGKREIMQLVAPAGPMYQAGTLSGNPLAMTAGIKTLELLRQPATYEYLDQITKRLSDGLLAIAQETGHAACGGQVSGMFGFFFTEGPVHNYEDAKKSDLQKFSRFHRGMLEQGIYLAPSQFEAGFTSLAHTEEDIDATLAAARTVMSAL  433
               SCOP domains d3fqaa_ A: automated matches                                                                                                                                                                                                                                                                                                                                                                                                               SCOP domains
               CATH domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ CATH domains
               Pfam domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ Pfam domains
         Sec.struct. author .hhhhhhhhhhhhhhhhhhh.hhhhhhhhhh.....eeeee..eeee....eeee.hhhhh.......hhhhhhhhhhhhh........hhhhhhhhhhhhhhh....eeeee.hhhhhhhhhhhhhhhhhh..eeeee.......hhhhh...hhhhhhh........hhhhhh.eeee...hhhhhhhhhhhh...eeeeee..............hhhhhhhhhhhhh..eeeee..........hhhhhhh.....eeeehhhhhh....eeeeehhhhhh................hhhhhhhhhhhhhhhh..hhhhhhhhhhhhhhhhhhhhhhhh....eeeee..eeeee.......hhhhhh..hhhhhhhhhhhhhhh.ee........ee.....hhhhhhhhhhhhhhhhhh. Sec.struct. author
                 SAPs(SNPs) ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ SAPs(SNPs)
                    PROSITE ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------AA_TRANSFER_CLASS_3  PDB: A:1242-1278----------------------------------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ Transcript
                3fqa A 1008 KTIKSDEIFAAAQKLMPGGVSSPVRAFKSVGGQPIVFDRVKDAYAWDVDGNRYIDYVGTWGPAICGHAHPEVIEALKVAMEKGTSFGAPCALENVLAEMVNDAVPSIEMVRFVNSGTEACMAVLRLMRAYTGRDKIIKFEGCYHGHADMFLVKAGSGVATLGLPSSPGVPKKTTANTLTTPYNDLEAVKALFAENPGEIAGVILEPIVGNSGFIVPDAGFLEGLREITLEHDALLVFDEVITGFRIAYGGVQEKFGVTPDLTTLGKIIGGGLPVGAYGGKREIMQLVAPAGPMYQAGTLSGNPLAMTAGIKTLELLRQPGTYEYLDQITKRLSDGLLAIAQETGHAACGGQVSGMFGFFFTEGPVHNYEDAKKSDLQKFSRFHRGMLEQGIYLAPSQFEAGFTSLAHTEEDIDATLAAARTVMSAL 1433
                                  1017      1027      1037      1047      1057      1067      1077      1087      1097      1107      1117      1127      1137      1147      1157      1167      1177      1187      1197      1207      1217      1227      1237      1247      1257      1267      1277      1287      1297      1307      1317      1327      1337      1347      1357      1367      1377      1387      1397      1407      1417      1427

Chain B from PDB  Type:PROTEIN  Length:426
 aligned with GSA_SYNP6 | P24630 from UniProtKB/Swiss-Prot  Length:433

    Alignment length:426
                                    17        27        37        47        57        67        77        87        97       107       117       127       137       147       157       167       177       187       197       207       217       227       237       247       257       267       277       287       297       307       317       327       337       347       357       367       377       387       397       407       417       427      
           GSA_SYNP6      8 KTIKSDEIFAAAQKLMPGGVSSPVRAFKSVGGQPIVFDRVKDAYAWDVDGNRYIDYVGTWGPAICGHAHPEVIEALKVAMEKGTSFGAPCALENVLAEMVIDAVPSIEMVRFVNSGTEACMAVLRLMRAYTGRDKIIKFEGCYHGHADMFLVKAGSGVATLGLPDSPGVPKSTTANTLTAPYNDLEAVKALFAENPGEIAGVILEPIVGNSGFIVPDAGFLEGLREITLEHDALLVFDEVMTGFRIAYGGVQEKFGVTPDLTTLGKIIGGGLPVGAYGGKREIMQLVAPAGPMYQAGTLSGNPLAMTAGIKTLELLRQPATYEYLDQITKRLSDGLLAIAQETGHAACGGQVSGMFGFFFTEGPVHNYEDAKKSDLQKFSRFHRGMLEQGIYLAPSQFEAGFTSLAHTEEDIDATLAAARTVMSAL  433
               SCOP domains d3fqab_ B: automated matches                                                                                                                                                                                                                                                                                                                                                                                                               SCOP domains
               CATH domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ CATH domains
               Pfam domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ Pfam domains
         Sec.struct. author .hhhhhhhhhhhhhhhhhhh.hhhhhh.........eeeee..eeee....eeee.hhhhh.......hhhhhhhhhhhhhhh......hhhhhhhhhhhhhhh....eeeee.hhhhhhhhhhhhhhhhhh..eeeee.......hhhhh...hhhhhhh..........hhhh.eeee...hhhhhhhhhhhh...eeeeee..............hhhhhhhhhhhhh..eeeee..........hhhhhhh.....eeeehhhhhh....eeeeehhhhhh................hhhhhhhhhhhhhhhh..hhhhhhhhhhhhhhhhhhhhhhhh....eeeee..eeeee.......hhhhhh..hhhhhhhhhhhhhhh.ee........ee.....hhhhhhhhhhhhhhhhhh. Sec.struct. author
                 SAPs(SNPs) ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ SAPs(SNPs)
                    PROSITE ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------AA_TRANSFER_CLASS_3  PDB: B:2242-2278----------------------------------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ Transcript
                3fqa B 2008 KTIKSDEIFAAAQKLMPGGVSSPVRAFKSVGGQPIVFDRVKDAYAWDVDGNRYIDYVGTWGPAICGHAHPEVIEALKVAMEKGTSFGAPCALENVLAEMVNDAVPSIEMVRFVNSGTEACMAVLRLMRAYTGRDKIIKFEGCYHGHADMFLVKAGSGVATLGLPSSPGVPKKTTANTLTTPYNDLEAVKALFAENPGEIAGVILEPIVGNSGFIVPDAGFLEGLREITLEHDALLVFDEVITGFRIAYGGVQEKFGVTPDLTTLGKIIGGGLPVGAYGGKREIMQLVAPAGPMYQAGTLSGNPLAMTAGIKTLELLRQPGTYEYLDQITKRLSDGLLAIAQETGHAACGGQVSGMFGFFFTEGPVHNYEDAKKSDLQKFSRFHRGMLEQGIYLAPSQFEAGFTSLAHTEEDIDATLAAARTVMSAL 2433
                                  2017      2027      2037      2047      2057      2067      2077      2087      2097      2107      2117      2127      2137      2147      2157      2167      2177      2187      2197      2207      2217      2227      2237      2247      2257      2267      2277      2287      2297      2307      2317      2327      2337      2347      2357      2367      2377      2387      2397      2407      2417      2427

Legend:		→ Mismatch	(orange background)
	-	→ Gap	(green background, '-', border residues have a numbering label)
		→ Modified Residue	(blue background, lower-case, 'x' indicates undefined single-letter code, labelled with number + name)
	x	→ Chemical Group	(purple background, 'x', labelled with number + name, e.g. ACE or NH2)
	extra numbering lines below/above indicate numbering irregularities and modified residue names etc., number ends below/above '\|'

Asymmetric/Biological Unit

Classes(

)

Folds(

)

Superfamilies( (-)

)

Families(

)

Protein Domains( (-)

)

Organisms( (-)

)

Class: Alpha and beta proteins (a/b) (23833)

Fold: PLP-dependent transferase-like (627)

Superfamily: PLP-dependent transferases (625)

Family: GABA-aminotransferase-like (167)

Protein domain: automated matches (28)

Synechococcus elongatus [TaxId: 269084] (8)

1a	d3fqaa_	A:
1b	d3fqab_	B:

(no "CATH Domain" information available for 3FQA)

(no "Pfam Domain" information available for 3FQA)

Asymmetric/Biological Unit(hide GO term definitions)

Chain A,B (GSA_SYNP6 | P24630)

molecular function
	GO:0003824	catalytic activity	Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
	GO:0042286	glutamate-1-semialdehyde 2,1-aminomutase activity	Catalysis of the reaction: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate.
	GO:0016853	isomerase activity	Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5.
	GO:0030170	pyridoxal phosphate binding	Interacting selectively and non-covalently with pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
	GO:0008483	transaminase activity	Catalysis of the transfer of an amino group to an acceptor, usually a 2-oxo acid.
biological process
	GO:0015995	chlorophyll biosynthetic process	The chemical reactions and pathways resulting in the formation of chlorophyll, any compound of magnesium complexed in a porphyrin (tetrapyrrole) ring and which functions as a photosynthetic pigment, from less complex precursors.
	GO:0006779	porphyrin-containing compound biosynthetic process	The chemical reactions and pathways resulting in the formation of any member of a large group of derivatives or analogs of porphyrin. Porphyrin consists of a ring of four pyrrole nuclei linked each to the next at their alpha positions through a methine group.
	GO:0006782	protoporphyrinogen IX biosynthetic process	The chemical reactions and pathways resulting in the formation of protoporphyrinogen IX.
	GO:0033014	tetrapyrrole biosynthetic process	The chemical reactions and pathways leading to the formation of tetrapyrroles, natural pigments containing four pyrrole rings joined by one-carbon units linking position 2 of one pyrrole ring to position 5 of the next.
cellular component
	GO:0005737	cytoplasm	All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

Asymmetric/Biological Unit
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	Cis Peptide Bonds
		Ala A:1295 - Pro A:1296	[ RasMol ]
		Ala B:2295 - Pro B:2296	[ RasMol ]
		Gly A:1370 - Pro A:1371	[ RasMol ]
		Gly B:2370 - Pro B:2371	[ RasMol ]
		Ser B:2173 - Pro B:2174	[ RasMol ]

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UniProtKB/Swiss-Prot
	GSA_SYNP6 \| P24630	:	2gsa 2hoy 2hoz 2hp1 2hp2 3fq7 3fq8 3gsb 4gsa

2hp1	DOUBLE PLP-FORM OF GSAM
2hp2	WILD TYPE FORM OF GSAM
3fq7	GABACULINE COMPLEX OF GSAM
3fq8	GABACULINE RESISTANT FORM OF GSAM

Description

Compounds

Structural Features

Chains, Units

Ligands, Modified Residues, Ions (2, 3)

Sites (3, 3)

SS Bonds (0, 0)

Cis Peptide Bonds (5, 5)

Sequence-Structure Mapping

SAPs(SNPs)/Variants (0, 0)

PROSITE Motifs (1, 2)

Exons (0, 0)

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Gene Ontology (10, 10)

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