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首页> 外文期刊>Nucleic Acids Research >Mycobacterial DNA polymerase I: activities and crystal structures of the POL domain as apoenzyme and in complex with a DNA primer-template and of the full-length FEN/EXO POL enzyme
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Mycobacterial DNA polymerase I: activities and crystal structures of the POL domain as apoenzyme and in complex with a DNA primer-template and of the full-length FEN/EXO POL enzyme

机译：分枝杆菌DNA聚合酶I：POL结构域的活性和晶体结构作为雌性瘤和与DNA引物 - 模板和全长FEN / EXO POL酶的复合物

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摘要

Mycobacterial Pol1 is a bifunctional enzyme composed of an N-terminal DNA flap endonuclease/5' exonuclease domain (FEN/EXO) and a C-terminal DNA polymerase domain (POL). Here we document additional functions of Pol1: FEN activity on the flap RNA strand of an RNA:DNA hybrid and reverse transcriptase activity on a DNA-primed RNA template. We report crystal structures of the POL domain, as apoenzyme and as ternary complex with 3'-dideoxy-terminated DNA primer-template and dNTP. The thumb, palm, and fingers subdomains of POL form an extensive interface with the primer-template and the triphosphate of the incoming dNTP. Progression from an open conformation of the apoenzyme to a nearly closed conformation of the ternary complex entails a disordered-to-ordered transition of several segments of the thumb and fingers modules and an inward motion of the fingers subdomain-especially the O helix-to engage the primer-template and dNTP triphosphate. Distinctive structural features of mycobacterial Pol1 POL include a manganese binding site in the vestigial 3' exonuclease subdomain and a non-catalytic water-bridged magnesium complex at the protein-DNA interface. We report a crystal structure of the bifunctional FEN/EXO-POL apoenzyme that reveals the positions of two active site metals in the FEN/EXO domain.
机译：分枝杆菌pol1是由N-末端DNA瓣内切核酸酶/ 5'外核酸酶结构域（FEN / EXO）和C末端DNA聚合酶（POL）组成的双官能酶。在这里，我们记录POL1：FEN活性的额外功能：在RNA的襟翼RNA链上的FEN活性：DNA杂交和逆转录酶活性在DNA - 灌注的RNA模板上。我们将Pol结构域的晶体结构报告为雌性瘤和作为三元复合物，与3'-二脱氧终止的DNA引物 - 模板和DNTP。 POL的拇指，手掌和手指子域与引物模板和进入的DNTP的三磷酸的大界面形成了广泛的界面。从缩进的开放构象的进展到三元复合物的几乎闭合的构象需要对拇指和手指模块的几个区段的若干段和手指子域外运动的无序转变 - 特别是o螺旋 - 以接​​合底漆模板和DNTP三磷酸酯。分枝杆菌POL1的独特结构特征在蛋白质-DNA界面处包括残留3'外切核酸酶亚域内的锰结合位点和非催化水桥镁络合物。我们报告了双功能FEN / EXO-POL孕义的晶体结构，揭示了FEN / EXO结构域中的两个活性位点金属的位置。

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