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PDBsum entry 3rmb
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Transferase/DNA
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PDB id
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3rmb
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PDB id:
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Transferase/DNA
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Title:
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Crystal structure of a replicative DNA polymerase bound to DNA containing thymine glycol
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Structure:
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DNA polymerase. Chain: a, b, c, d. Synonym: gp43. Engineered: yes. Mutation: yes. DNA (5'-d( Cp Gp Cp (Ctg) p Gp Ap Ap Tp Gp Ap Cp Ap Gp Cp Cp Gp Cp G)-3'). Chain: e, g, i, k. Engineered: yes.
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Source:
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Enterobacteria phage rb69. Organism_taxid: 12353. Gene: 43, gp43. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Synthetic: yes
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Resolution:
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2.65Å
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R-factor:
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0.224
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R-free:
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0.276
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Authors:
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P.Aller,S.Duclos,S.S.Wallace,S.Doublie
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Key ref:
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P.Aller
et al.
(2011).
A crystallographic study of the role of sequence context in thymine glycol bypass by a replicative DNA polymerase serendipitously sheds light on the exonuclease complex.
J Mol Biol,
412,
22-34.
PubMed id:
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Date:
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20-Apr-11
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Release date:
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10-Aug-11
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PROCHECK
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Headers
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References
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Q38087
(DPOL_BPR69) -
DNA-directed DNA polymerase from Escherichia phage RB69
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Seq:
Struc:
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903 a.a.
903 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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C-G-C-CTG-G-A-A-T-G-A-C-A-G-C-C-G-C-G
18 bases
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G-C-G-G-C-T-G-T-C-A-T-T-C-A
14 bases
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C-G-C-CTG-G-A-A-T-G-A-C-A-G-C-C-G-C-G
18 bases
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G-C-G-G-C-T-G-T-C-A-T-T-C-A
14 bases
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C-G-C-CTG-G-A-A-T-G-A-C-A-G-C-C-G-C-G
18 bases
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G-C-G-G-C-T-G-T-C-A-T-T-C-A
14 bases
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C-G-C-CTG-G-A-A-T-G-A-C-A-G-C-C-G-C-G
18 bases
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G-C-G-G-C-T-G-T-C-A-T-T-C-A
14 bases
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Enzyme class:
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E.C.2.7.7.7
- DNA-directed Dna polymerase.
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Reaction:
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DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate
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DNA(n)
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+
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2'-deoxyribonucleoside 5'-triphosphate
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=
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DNA(n+1)
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+
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diphosphate
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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J Mol Biol
412:22-34
(2011)
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PubMed id:
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A crystallographic study of the role of sequence context in thymine glycol bypass by a replicative DNA polymerase serendipitously sheds light on the exonuclease complex.
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P.Aller,
S.Duclos,
S.S.Wallace,
S.Doublié.
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ABSTRACT
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Links
