Structural highlights
Function
DPOL_BPR69 This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction.
Publication Abstract from PubMed
Recent structures of DNA polymerase complexes with dGMPCPP/dT and dCTP/dA mispairs at the insertion site have shown that they adopt Watson-Crick geometry in the presence of Mn2+ indicating that the tautomeric or ionization state of the base has changed. To see whether the tautomeric or ionization state of base-pair could be affect by its microenvironment, we determined ten structures of an RB69 DNA polymerase quadruple mutant with dG/dT or dT/dG mispairs at position n-1 to n-5 of the Primer/Template duplex. Different shapes of the mispairs, including Watson-Crick geometry, have been observed, strongly suggesting that the local environment of base-pairs plays an important role in their tautomeric or ionization states.
Mispairs with Watson-Crick Base-pair Geometry Observed in Ternary Complexes of an RB69 DNA Polymerase Variant.,Xia S, Konigsberg WH Protein Sci. 2014 Jan 24. doi: 10.1002/pro.2434. PMID:24458997[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xia S, Konigsberg WH. Mispairs with Watson-Crick Base-pair Geometry Observed in Ternary Complexes of an RB69 DNA Polymerase Variant. Protein Sci. 2014 Jan 24. doi: 10.1002/pro.2434. PMID:24458997 doi:http://dx.doi.org/10.1002/pro.2434
