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(-) Description

Title :  CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THE WILD-TYPE LACTOCOCCUS LACTIS FPG (MUTM) AND A N7-BENZYL-FAPY-DG CONTAINING DNA
 
Authors :  F. Coste, B. Castaing, T. Carell
Date :  31 Jan 08  (Deposition) - 16 Dec 08  (Release) - 13 Jul 11  (Revision)
Method :  X-RAY DIFFRACTION
Resolution :  1.90
Chains :  Asym./Biol. Unit :  A,B,C
Keywords :  Protein-Dna Complex, Glycosylase, Benzyl-Fapy, Dna Repair, Hydrolase- Dna Complex, Dna Damage, Dna-Binding, Glycosidase, Lyase, Metal- Binding, Multifunctional Enzyme, Zinc-Finger (Keyword Search: [Gene Ontology, PubMed, Web (Google))
 
Reference :  F. Coste, M. Ober, Y. V. Le Bihan, M. A. Izquierdo, N. Hervouet, H. Mueller, T. Carell, B. Castaing
Bacterial Base Excision Repair Enzyme Fpg Recognizes Bulky N7-Substituted-Fapydg Lesion Via Unproductive Binding Mode
Chem. Biol. V. 15 706 2008
PubMed-ID: 18635007  |  Reference-DOI: 10.1016/J.CHEMBIOL.2008.05.014

(-) Compounds

Molecule 1 - DNA GLYCOSYLASE
    ChainsA
    EC Number4.2.99.18
    EngineeredYES
    Expression SystemESCHERICHIA COLI
    Expression System PlasmidPMAL-C
    Expression System StrainBL21
    Expression System Taxid562
    Expression System Vector TypePLASMID
    GeneMUTM, FPG
    Organism ScientificLACTOCOCCUS LACTIS
    Organism Taxid416870
    SynonymFAPY-DNA GLYCOSYLASE, DNA-APURINIC OR APYRIMIDINIC SITE, LYASE MUTM, AP LYASE MUTM
    VariantSUBSP. CREMORIS
 
Molecule 2 - DNA (5'-D(*DCP*DTP*DCP*DTP*DTP*DTP*(SOS) P*DTP*DTP*DTP*DCP*DTP*DCP*DG)-3')
    ChainsB
    EngineeredYES
    Other DetailsSYNTHETIC DNA
    SyntheticYES
 
Molecule 3 - DNA (5'- D(*DGP*DCP*DGP*DAP*DGP*DAP*DAP*DAP*DCP*DAP*DAP*DAP*DGP*DA)-3')
    ChainsC
    EngineeredYES
    Other DetailsSYNTHETIC DNA
    SyntheticYES

 Structural Features

(-) Chains, Units

  123
Asymmetric/Biological Unit ABC

Summary Information (see also Sequences/Alignments below)

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

Asymmetric/Biological Unit (3, 3)
No.NameCountTypeFull Name
1GOL1Ligand/IonGLYCEROL
2SOS1Mod. Nucleotide[(1R,2S,4R)-4-({2-AMINO-5-[BENZYL(FORMYL)AMINO]-6-OXO-1,6-DIHYDROPYRIMIDIN-4-YL}AMINO)-2-HYDROXYCYCLOPENTYL]METHYL DIHYDROGEN PHOSPHATE
3ZN1Ligand/IonZINC ION

(-) Sites  (3, 3)

Asymmetric Unit (3, 3)
No.NameEvidenceResiduesDescription
1AC1SOFTWAREPRO A:1 , GLU A:2 , GLU A:5 , MET A:75 , ASN A:171 , ILE A:172 , SER A:217 , ILE A:219 , TYR A:238 , ARG A:260 , DT B:6 , DT B:8BINDING SITE FOR RESIDUE SOS B 7
2AC2SOFTWARECYS A:245 , CYS A:248 , CYS A:265 , CYS A:268BINDING SITE FOR RESIDUE ZN A 401
3AC3SOFTWARETYR A:58 , HIS A:72 , ARG A:74 , THR A:113 , GLU A:115 , TYR A:125 , LYS A:129 , DT B:9 , DT B:10BINDING SITE FOR RESIDUE GOL A 402

(-) SS Bonds  (0, 0)

(no "SS Bond" information available for 3C58)

(-) Cis Peptide Bonds  (0, 0)

(no "Cis Peptide Bond" information available for 3C58)

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 3C58)

(-) PROSITE Motifs  (3, 3)

Asymmetric/Biological Unit (3, 3)
 PROSITEUniProtKBPDB
No.IDACDescriptionIDLocationCountLocation
1FPG_CATPS51068 Formamidopyrimidine-DNA glycosylase catalytic domain profile.FPG_LACLC2-113  1A:1-112
2ZF_FPG_2PS51066 Zinc finger FPG-type profile.FPG_LACLC238-272  1A:236-270
3ZF_FPG_1PS01242 Zinc finger FPG-type signature.FPG_LACLC247-271  1A:245-269

(-) Exons   (0, 0)

(no "Exon" information available for 3C58)

(-) 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:269
 aligned with FPG_LACLC | P42371 from UniProtKB/Swiss-Prot  Length:273

    Alignment length:272
                                    11        21        31        41        51        61        71        81        91       101       111       121       131       141       151       161       171       181       191       201       211       221       231       241       251       261       271  
            FPG_LACLC     2 PELPEVETVRRELEKRIVGQKIISIEATYPRMVLTGFEQLKKELTGKTIQGISRRGKYLIFEIGDDFRLISHLRMEGKYRLATLDAPREKHDHLTMKFADGQLIYADVRKFGTWELISTDQVLPYFLKKKIGPEPTYDEDFDEKLFREKLRKSTKKIKPYLLEQTLVAGLGNIYVDEVLWLAKIHPEKETNQLIESSIHLLHDSIIEILQKAIKLGGSSIRTYSALGSTGKMQNELQVYGKTGEKCSRCGAEIQKIKVAGRGTHFCPVCQQK 273
               SCOP domains -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author .hhhhhhhhhhhhhhhhh.....eeee.hhhhh..hhhhhhhhhh...eeeeeee..eeeeee...eeeeee.....eeeee.........eeeeee....eeeee......eeeeee..hhhhhhhhhh.......-...hhhhhhhhhhh...hhhhhhhh.......hhhhhhhhhhhh......hhhhhhhhhhhhhhhhhhhhhhhhhhh......--.......hhhhhh.................eeeee..eeeee....... Sec.struct. author
                 SAPs(SNPs) -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                PROSITE (1) FPG_CAT  PDB: A:1-112 UniProt: 2-113                                                                            ----------------------------------------------------------------------------------------------------------------------------ZF_FPG_2  PDB: A:236-270           - PROSITE (1)
                PROSITE (2) -----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ZF_FPG_1  PDB: A:245-269 -- PROSITE (2)
                 Transcript -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 3c58 A   1 PELPEVETVRRELEKRIVGQKIISIEATYPRMVLTGFEQLKKELTGKTIQGISRRGKYLIFEIGDDFRLISHLRMEGKYRLATLDAPREKHDHLTMKFADGQLIYADVRKFGTWELISTDQVLPYFLKKKIGPEPTY-EDFDEKLFREKLRKSTKKIKPYLLEQTLVAGLGNIYVDEVLWLAKIHPEKETNQLIESSIHLLHDSIIEILQKAIKLGGSSIR--SALGSTGKMQNELQVYGKTGEKCSRCGAEIQKIKVAGRGTHFCPVCQQK 271
                                    10        20        30        40        50        60        70        80        90       100       110       120       130      |139       149       159       169       179       189       199       209       219|  |   229       239       249       259       269  
                                                                                                                                                                  137 |                                                                               220  |                                                
                                                                                                                                                                    138                                                                                  223                                                

Chain B from PDB  Type:DNA  Length:14
                                              
                 3c58 B   1 CTCTTTxTTTCTCG  14
                                  | 10    
                                  7-SOS   

Chain C from PDB  Type:DNA  Length:14
                                              
                 3c58 C  15 GCGAGAAACAAAGA  28
                                    24    

   Legend:   → Mismatch (orange background)
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  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 3C58)

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 3C58)

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 3C58)

(-) Gene Ontology  (17, 17)

Asymmetric/Biological Unit(hide GO term definitions)
Chain A   (FPG_LACLC | P42371)
molecular function
    GO:0003677    DNA binding    Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
    GO:0003906    DNA-(apurinic or apyrimidinic site) lyase activity    Catalysis of the cleavage of the C-O-P bond 3' to the apurinic or apyrimidinic site in DNA by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
    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:0003684    damaged DNA binding    Interacting selectively and non-covalently with damaged DNA.
    GO:0016787    hydrolase activity    Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3.
    GO:0016798    hydrolase activity, acting on glycosyl bonds    Catalysis of the hydrolysis of any glycosyl bond.
    GO:0016799    hydrolase activity, hydrolyzing N-glycosyl compounds    Catalysis of the hydrolysis of any N-glycosyl bond.
    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.
    GO:0046872    metal ion binding    Interacting selectively and non-covalently with any metal ion.
    GO:0003676    nucleic acid binding    Interacting selectively and non-covalently with any nucleic acid.
    GO:0008534    oxidized purine nucleobase lesion DNA N-glycosylase activity    Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme-substrate intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apurinic (AP) site.
    GO:0008270    zinc ion binding    Interacting selectively and non-covalently with zinc (Zn) ions.
biological process
    GO:0006281    DNA repair    The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
    GO:0006284    base-excision repair    In base excision repair, an altered base is removed by a DNA glycosylase enzyme, followed by excision of the resulting sugar phosphate. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase.
    GO:0006974    cellular response to DNA damage stimulus    Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
    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.
    GO:0006289    nucleotide-excision repair    A DNA repair process in which a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts).

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 Related Entries

(-) Entries Sharing at Least One Protein Chain (UniProt ID)

UniProtKB/Swiss-Prot
        FPG_LACLC | P423711kfv 1nnj 1pji 1pjj 1pm5 1tdz 1xc8 2xzf 2xzu 4pcz 4pd2 4pdg 4pdi

(-) Related Entries Specified in the PDB File

(no "Related Entries Specified in the PDB File" available for 3C58)