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4IRD

Structure of Polymerase-DNA complex

Summary for 4IRD
Entry DOI10.2210/pdb4ird/pdb
Related4IR1 4IR9 4IRC 4IRK
DescriptorDNA (5'-D(*TP*CP*TP*TP*GP*GP*GP*TP*CP*CP*TP*AP*GP*GP*AP*CP*CP*C)-3'), DNA (5'-D(*GP*GP*GP*TP*CP*CP*TP*AP*GP*GP*AP*CP*CP*C)-3'), DNA (5'-D(*CP*TP*AP*GP*GP*GP*TP*CP*CP*TP*AP*GP*GP*AP*CP*CP*C)-3'), ... (7 entities in total)
Functional Keywordsdna polymerase, y-family, transferase-dna complex, transferase/dna
Biological sourceEscherichia coli
Cellular locationCytoplasm (Probable): Q47155
Total number of polymer chains6
Total formula weight98123.39
Authors
Nair, D.T.,Sharma, A. (deposition date: 2013-01-14, release date: 2013-04-10, Last modification date: 2024-02-28)
Primary citationSharma, A.,Kottur, J.,Narayanan, N.,Nair, D.T.
A strategically located serine residue is critical for the mutator activity of DNA polymerase IV from Escherichia coli.
Nucleic Acids Res., 41:5104-5114, 2013
Cited by
PubMed Abstract: The Y-family DNA polymerase IV or PolIV (Escherichia coli) is the founding member of the DinB family and is known to play an important role in stress-induced mutagenesis. We have determined four crystal structures of this enzyme in its pre-catalytic state in complex with substrate DNA presenting the four possible template nucleotides that are paired with the corresponding incoming nucleotide triphosphates. In all four structures, the Ser42 residue in the active site forms interactions with the base moieties of the incipient Watson-Crick base pair. This residue is located close to the centre of the nascent base pair towards the minor groove. In vitro and in vivo assays show that the fidelity of the PolIV enzyme increases drastically when this Ser residue was mutated to Ala. In addition, the structure of PolIV with the mismatch A:C in the active site shows that the Ser42 residue plays an important role in stabilizing dCTP in a conformation compatible with catalysis. Overall, the structural, biochemical and functional data presented here show that the Ser42 residue is present at a strategic location to stabilize mismatches in the PolIV active site, and thus facilitate the appearance of transition and transversion mutations.
PubMed: 23525461
DOI: 10.1093/nar/gkt146
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.48 Å)
Structure validation

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건을2024-11-06부터공개중

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