Structure of the catalytic core of S-cerevisiae DNA polymerase η:: Implications for translesion DNA synthesis
Structure of the catalytic core of S-cerevisiae DNA polymerase η:: Implications for translesion DNA synthesis
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DOI：
10.1016/s1097-2765(01)00306-9
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发表时间：
2001-08-01
期刊：
影响因子：
16
通讯作者：
Aggarwal, AK
中科院分区：
文献类型：
--
作者：
Trincao, J;Johnson, RE;Aggarwal, AK
DNA聚合酶eta在真核生物聚合酶中是独特的，其熟练的复制能力通过各种扭曲的DNA损伤。本文报道了S催化核的晶体结构。酿酒酵母DNA聚合酶eta，在2.25埃分辨率下测定。该结构揭示了一种新的多指右手形分子与一个独特的聚合酶相关的结构域。我们鉴定了催化残基，并表明手指和拇指结构域异常小且短。特别是，螺旋“O”和“O 1”的手指结构域中的意外的情况下，表明开放的活性位点是关键的功能，使DNA聚合酶eta复制通过DNA损伤，如紫外线诱导的顺式胸腺嘧啶-胸腺嘧啶二聚体。
DNA polymerase eta is unique among eukaryotic polymerases in its proficient ability to replicate through a variety of distorting DNA lesions. We report here the crystal structure of the catalytic core of S. cerevisiae DNA polymerase eta, determined at 2.25 Angstrom resolution. The structure reveals a novel polydactyl right hand shaped molecule with a unique polymerase-associated domain. We identify the catalytic residues and show that the fingers and thumb domains are unusually small and stubby. In particular, the unexpected absence of helices "O" and "O1" in the fingers domain suggests that openness of the active site is the critical feature which enables DNA polymerase eta to replicate through DNA lesions such as a UV-induced cis-syn thymine-thymine dimer.