Literature DB >> 22238207

Bidentate and tridentate metal-ion coordination states within ternary complexes of RB69 DNA polymerase.

Shuangluo Xia1, Soo Hyun Eom, William H Konigsberg, Jimin Wang.   

Abstract

Two divalent metal ions are required for primer-extension catalyzed by DNA polymerases. One metal ion brings the 3'-hydroxyl of the primer terminus and the α-phosphorus atom of incoming dNTP together for bond formation so that the catalytically relevant conformation of the triphosphate tail of the dNTP is in an α,β,γ-tridentate coordination complex with the second metal ion required for proper substrate alignment. A probable base selectivity mechanism derived from structural studies on Dpo4 suggests that the inability of mispaired dNTPs to form a substrate-aligned, tridentate coordination complex could effectively cause the mispaired dNTPs to be rejected before catalysis. Nevertheless, we found that mispaired dNTPs can actually form a properly aligned tridentate coordination complex. However, complementary dNTPs occasionally form misaligned complexes with mutant RB69 DNA polymerases (RB69pols) that are not in a tridentate coordination state. Here, we report finding a β,γ-bidentate coordination complex that contained the complementary dUpNpp opposite dA in the structure of a ternary complex formed by the wild type RB69pol at 1.88 Å resolution. Our observations suggest that several distinct metal-ion coordination states can exist at the ground state in the polymerase active site and that base selectivity is unlikely to be based on metal-ion coordination alone.
Copyright © 2012 The Protein Society.

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Year:  2012        PMID: 22238207      PMCID: PMC3375444          DOI: 10.1002/pro.2026

Source DB:  PubMed          Journal:  Protein Sci        ISSN: 0961-8368            Impact factor:   6.725


  17 in total

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4.  The structure of a high fidelity DNA polymerase bound to a mismatched nucleotide reveals an "ajar" intermediate conformation in the nucleotide selection mechanism.

Authors:  Eugene Y Wu; Lorena S Beese
Journal:  J Biol Chem       Date:  2011-03-19       Impact factor: 5.157

5.  Fidelity of Dpo4: effect of metal ions, nucleotide selection and pyrophosphorolysis.

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Journal:  EMBO J       Date:  2005-08-18       Impact factor: 11.598

6.  Structures of DNA polymerase beta with active-site mismatches suggest a transient abasic site intermediate during misincorporation.

Authors:  Vinod K Batra; William A Beard; David D Shock; Lars C Pedersen; Samuel H Wilson
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7.  The reopening rate of the fingers domain is a determinant of base selectivity for RB69 DNA polymerase.

Authors:  Harold R Lee; Mina Wang; William Konigsberg
Journal:  Biochemistry       Date:  2009-03-17       Impact factor: 3.162

8.  RB69 DNA polymerase mutants with expanded nascent base-pair-binding pockets are highly efficient but have reduced base selectivity.

Authors:  Hong Zhang; Jeff Beckman; Jimin Wang; William Konigsberg
Journal:  Biochemistry       Date:  2009-07-28       Impact factor: 3.162

9.  Insights into base selectivity from the 1.8 Å resolution structure of an RB69 DNA polymerase ternary complex.

Authors:  Mina Wang; Shuangluo Xia; Gregor Blaha; Thomas A Steitz; William H Konigsberg; Jimin Wang
Journal:  Biochemistry       Date:  2010-12-30       Impact factor: 3.162

10.  Phaser crystallographic software.

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  6 in total

1.  Using a fluorescent cytosine analogue tC(o) to probe the effect of the Y567 to Ala substitution on the preinsertion steps of dNMP incorporation by RB69 DNA polymerase.

Authors:  Shuangluo Xia; Jeff Beckman; Jimin Wang; William H Konigsberg
Journal:  Biochemistry       Date:  2012-05-22       Impact factor: 3.162

2.  Probing minor groove hydrogen bonding interactions between RB69 DNA polymerase and DNA.

Authors:  Shuangluo Xia; Thomas D Christian; Jimin Wang; William H Konigsberg
Journal:  Biochemistry       Date:  2012-05-17       Impact factor: 3.162

3.  Molecular events during translocation and proofreading extracted from 200 static structures of DNA polymerase.

Authors:  Zhong Ren
Journal:  Nucleic Acids Res       Date:  2016-06-20       Impact factor: 16.971

Review 4.  Filovirus proteins for antiviral drug discovery: A structure/function analysis of surface glycoproteins and virus entry.

Authors:  Baptiste Martin; Thomas Hoenen; Bruno Canard; Etienne Decroly
Journal:  Antiviral Res       Date:  2016-09-14       Impact factor: 5.970

5.  Alteration in the cavity size adjacent to the active site of RB69 DNA polymerase changes its conformational dynamics.

Authors:  Shuangluo Xia; Marcus Wood; Michael J Bradley; Enrique M De La Cruz; William H Konigsberg
Journal:  Nucleic Acids Res       Date:  2013-08-05       Impact factor: 16.971

Review 6.  RB69 DNA polymerase structure, kinetics, and fidelity.

Authors:  Shuangluo Xia; William H Konigsberg
Journal:  Biochemistry       Date:  2014-04-23       Impact factor: 3.162

  6 in total

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