克莱诺碎片
DNA聚合酶Ⅰ
DNA聚合酶
DNA钳
DNA聚合酶Ⅱ
底漆(化妆品)
碱基对
聚合酶
核酸外切酶
初级
生物
DNA
分子生物学
复式(建筑)
化学
遗传学
逆转录酶
聚合酶链反应
基因
有机化学
作者
L.S. Beese,Victoria Derbyshire,Thomas A. Steitz
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:1993-04-16
卷期号:260 (5106): 352-355
被引量:462
标识
DOI:10.1126/science.8469987
摘要
Klenow fragment of Escherichia coli DNA polymerase I, which was cocrystallized with duplex DNA, positioned 11 base pairs of DNA in a groove that lies at right angles to the cleft that contains the polymerase active site and is adjacent to the 3′ to 5′ exonuclease domain. When the fragment bound DNA, a region previously referred to as the "disordered domain" became more ordered and moved along with two helices toward the 3′ to 5′ exonuclease domain to form the binding groove. A single-stranded, 3′ extension of three nucleotides bound to the 3′ to 5′ exonuclease active site. Although this cocrystal structure appears to be an editing complex, it suggests that the primer strand approaches the catalytic site of the polymerase from the direction of the 3′ to 5′ exonuclease domain and that the duplex DNA product may bend to enter the cleft that contains the polymerase catalytic site.
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