1TVA

HUMAN DNA POLYMERASE BETA COMPLEXED WITH NICKED DNA CONTAINING A MISMATCHED TEMPLATE THYMIDINE AND INCOMING CYTIDINE

Summary for 1TVA

• Entry DOI: 10.2210/pdb1tva/pdb
• Related: 1BPZ 1TV9
• Descriptor: 5'-D(*CP*CP*GP*AP*CP*TP*GP*CP*GP*CP*AP*TP*CP*AP*GP*C)-3', 5'-D(*GP*CP*TP*GP*AP*TP*GP*CP*GP*CP*C)-3', 5'-D(P*GP*TP*CP*GP*G)-3', ... (8 entities in total)
• Functional Keywords: nucleotidyltransferase, dna repair, dna mismatch, base excision repair, transferase-dna complex, transferase/dna
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P06746
• Total number of polymer chains: 4
• Total formula weight: 48161.60

Authors

Krahn, J.M.,Beard, W.A.,Wilson, S.H. (deposition date: 2004-06-29, release date: 2004-11-23, Last modification date: 2024-02-14)

Primary citation

Krahn, J.M.,Beard, W.A.,Wilson, S.H.
Structural insights into DNA polymerase Beta deterrents for misincorporation support an induced-fit mechanism for fidelity
Structure, 12:1823-1832, 2004

PubMed Abstract: DNA polymerases generally select the correct nucleotide from a pool of structurally similar molecules to preserve Watson-Crick base-pairing rules. We report the structure of DNA polymerase beta with DNA mismatches situated in the polymerase active site. This was achieved by using nicked product DNA that traps the mispair (template-primer, A-C or T-C) in the nascent base pair binding pocket. The structure of each mispair complex indicates that the bases do not form hydrogen bonds with one another, but form a staggered arrangement where the bases of the mispair partially overlap. This prevents closure/opening of the N subdomain that is believed to be required for catalytic cycling. The partially open conformation of the N subdomain results in distinct hydrogen bonding networks that are unique for each mispair. These structures define diverse molecular aspects of misinsertion that are consistent with the induced-fit model for substrate specificity.

PubMed: 15458631
DOI: 10.1016/j.str.2004.08.001

Experimental method

X-RAY DIFFRACTION (2.6 Å)