Structure and mechanism of DNA polymerase β.

Structure and mechanism of DNA polymerase β.
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DNA聚合酶β的结构和机制。

DOI:
10.1021/bi500139h
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发表时间:
2014-05-06
期刊:
影响因子:
2.9
通讯作者:
Wilson SH
Wilson SH
中科院分区:
生物学3区
文献类型:
--
作者:
Beard WA;Wilson SH

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DNA聚合酶(pol)β是一种由两个结构域组成的小分子真核生物DNA聚合酶。每个结构域在简单碱基损伤的修复过程中贡献酶活性(DNA合成和脱氧核糖磷酸裂解酶)。这些结构域分别称为聚合酶和裂解酶结构域。Pol β是研究核苷酸转移酶反应和底物识别的理想模型酶。本文综述了pol β在正确和错误的核苷酸插入过程中以及在损伤DNA(脱嘌呤位点和8-氧代鸟嘌呤)的旁路过程中处于各种配体和构象状态的晶体学研究。这些催化中间体的结构提供了意想不到的见解DNA聚合酶增强基因组稳定性的机制。这些结构还提供了一个改进的框架,允许计算研究,以促进解释详细的动力学分析,这种模型酶。
DNA polymerase (pol) β is a small eukaryotic DNA polymerase composed of two domains. Each domain contributes an enzymatic activity (DNA synthesis and deoxyribose phosphate lyase) during the repair of simple base lesions. These domains are termed the polymerase and lyase domains, respectively. Pol β has been an excellent model enzyme for studying the nucleotidyl transferase reaction and substrate discrimination at a molecular level. In this review, recent crystallographic studies of pol β in various liganded and conformational states during the insertion of right and wrong nucleotides as well as during the bypass of damaged DNA (apurinic sites and 8-oxoguanine) are described. Structures of these catalytic intermediates provide unexpected insights into mechanisms by which DNA polymerases enhance genome stability. These structures also provide an improved framework that permits computational studies to facilitate the interpretation of detailed kinetic analyses of this model enzyme.
DOI: 10.1016/s0921-8777(00)00029-x
发表时间: 2000-08-30
期刊: MUTATION RESEARCH-DNA REPAIR
影响因子: --
作者:
Beard, WA;Wilson, SH
通讯作者: Wilson, SH
DOI: 10.1016/j.str.2006.01.011
发表时间: 2006-04-01
期刊: STRUCTURE
影响因子: 5.7
作者:
Batra, VK;Beard, WA;Wilson, SH
通讯作者: Wilson, SH
DOI: 10.1074/jbc.m404016200
发表时间: 2004-07-23
影响因子: 4.8
作者:
Beard, WA;Shock, DD;Wilson, SH
通讯作者: Wilson, SH
DOI: 10.1093/nar/21.4.787
发表时间: 1993-02-25
影响因子: 14.9
作者:
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通讯作者: ITO, J
DOI: 10.1073/pnas.1112235108
发表时间: 2012-01-03
影响因子: 11.1
作者:
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通讯作者: Wilson, Samuel H.