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(-) Description

Title :  CRYSTAL STRUCTURE OF SMU.1381 (OR LEUD) FROM STREPTOCOCCUS MUTANS
 
Authors :  Z. Q. Gao, H. F. Hou, L. F. Li, Y. H. Liang, X. D. Su, Y. H. Dong
Date :  19 Jun 06  (Deposition) - 04 Jul 06  (Release) - 24 Feb 09  (Revision)
Method :  X-RAY DIFFRACTION
Resolution :  2.10
Chains :  Asym./Biol. Unit :  A
Keywords :  Beta Barrel, Lyase (Keyword Search: [Gene Ontology, PubMed, Web (Google))
 
Reference :  Z. Q. Gao, H. F. Hou, R. Xu, L. Q. Li, J. H. Xu, L. F. Li, Y. H. Liang, X. D. Su, P. Liu, Y. H. Dong
Crystal Structure Of Smu. 1381 (Or Leud) From Streptococcus Mutans
To Be Published
PubMed: search
(for further references see the PDB file header)

(-) Compounds

Molecule 1 - 3-ISOPROPYLMALATE DEHYDRATASE SMALL SUBUNIT
    ChainsA
    EC Number4.2.1.33
    EngineeredYES
    Expression SystemESCHERICHIA COLI BL21(DE3)
    Expression System PlasmidPET-28A
    Expression System StrainBL21(DE3)
    Expression System Taxid469008
    Expression System Vector TypePLASMID
    Organism ScientificSTREPTOCOCCUS MUTANS
    Organism Taxid1309
    SynonymISOPROPYLMALATE ISOMERASE, ALPHA-IPM ISOMERASE, IPMI

 Structural Features

(-) Chains, Units

  1
Asymmetric/Biological Unit A

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (1, 3)

Asymmetric/Biological Unit (1, 3)
No.NameCountTypeFull Name
1SO43Ligand/IonSULFATE ION

(-) Sites  (3, 3)

Asymmetric Unit (3, 3)
No.NameEvidenceResiduesDescription
1AC1SOFTWAREGLY A:37 , PHE A:38 , GLY A:39 , LYS A:40 , ASP A:93BINDING SITE FOR RESIDUE SO4 A 1001
2AC2SOFTWAREPRO A:123 , LYS A:124 , HOH A:1046BINDING SITE FOR RESIDUE SO4 A 1002
3AC3SOFTWAREASN A:16 , ASP A:17BINDING SITE FOR RESIDUE SO4 A 1003

(-) SS Bonds  (0, 0)

(no "SS Bond" information available for 2HCU)

(-) Cis Peptide Bonds  (0, 0)

(no "Cis Peptide Bond" information available for 2HCU)

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 2HCU)

(-) PROSITE Motifs  (0, 0)

(no "PROSITE Motif" information available for 2HCU)

(-) Exons   (0, 0)

(no "Exon" information available for 2HCU)

(-) Sequences/Alignments

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:177
 aligned with LEUD_STRMU | Q8DTG5 from UniProtKB/Swiss-Prot  Length:196

    Alignment length:177
                                 1                                                                                                                                                                           
                                 |   5        15        25        35        45        55        65        75        85        95       105       115       125       135       145       155       165       
           LEUD_STRMU     - -----MEEFTIYTGTTVPLMNDNIDTDQILPKQFLKLIDKKGFGKYLMYEWRYLDNNYTENPDFIFNQPEYREASILITGDNFGAGSSREHAAWALADYGFKVIVAGSFGDIHYNNDLNNGILPIIQPKEVRDKLAKLKPTDEVTVNLFEQKIYSPVGDFSFDIDGEWKHKLLNGLD 172
               SCOP domains --------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains --------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains --------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author ..........eeeeeeeee.....hhhhhhhhhhhhh.....hhhhhhhhhhh..........hhhhhhhhh...eeee.........hhhhhhhhhhhh..eeee...hhhhhhhhhh...eeee.hhhhhhhhhh.....eeeee....eeee..eeee...hhhhhhhhhh... Sec.struct. author
                 SAPs(SNPs) --------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE --------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript --------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 2hcu A  -4 MGRGSMEEFTIYTGTTVPLMNDNIDTDQILPKQFLKLIDKKGFGKYLMYEWRYLDNNYTENPDFIFNQPEYREASILITGDNFGAGSSREHAAWALADYGFKVIVAGSFGDIHYNNDLNNGILPIIQPKEVRDKLAKLKPTDEVTVNLFEQKIYSPVGDFSFDIDGEWKHKLLNGLD 172
                                     5        15        25        35        45        55        65        75        85        95       105       115       125       135       145       155       165       

   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 '|'

 Classification and Annotation

(-) SCOP Domains  (0, 0)

(no "SCOP Domain" information available for 2HCU)

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 2HCU)

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 2HCU)

(-) Gene Ontology  (7, 7)

Asymmetric/Biological Unit(hide GO term definitions)
Chain A   (LEUD_STRMU | Q8DTG5)
molecular function
    GO:0003861    3-isopropylmalate dehydratase activity    Catalysis of the reaction: 3-isopropylmalate = 2-isopropylmaleate + H2O.
    GO:0016829    lyase activity    Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.
biological process
    GO:0009082    branched-chain amino acid biosynthetic process    The chemical reactions and pathways resulting in the formation of amino acids containing a branched carbon skeleton, comprising isoleucine, leucine and valine.
    GO:0008652    cellular amino acid biosynthetic process    The chemical reactions and pathways resulting in the formation of amino acids, organic acids containing one or more amino substituents.
    GO:0009098    leucine biosynthetic process    The chemical reactions and pathways resulting in the formation of leucine, 2-amino-4-methylpentanoic acid.
    GO:0008152    metabolic process    The chemical reactions and pathways, including anabolism and catabolism, by which living organisms transform chemical substances. Metabolic processes typically transform small molecules, but also include macromolecular processes such as DNA repair and replication, and protein synthesis and degradation.
cellular component
    GO:0009316    3-isopropylmalate dehydratase complex    A heterodimeric enzyme complex composed of subunits leuC and leuD. Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.

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