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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of taq DNA polymerase shows a new orientation for the structure-specific nuclease domain.
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Structure of taq DNA polymerase shows a new orientation for the structure-specific nuclease domain.

机译：taq DNA聚合酶的结构显示一个新的取向的structure-specific核酸酶域。

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摘要

Thermus aquaticus DNA polymerase I consists of the polymerase, the structure-specific nuclease and the vestigial editing nuclease domains. Three-dimensional structures of the native enzyme and its complex with DNA have already been reported. The structure of a complex with an inhibitory antibody has also been determined. The structure of the native enzyme in a different crystal form determined at 2.6 A is reported here. Optimized anomalous diffraction measurements made at the holmium L(III) edge were valuable in validating solutions obtained through molecular replacement. The structure of the polymerase domain is similar to those reported previously, while the relative orientation of the structure-specific nuclease domain is significantly different from those of the native enzyme and the DNA complex; it is, however, identical to that observed in the structure of the Fab complex. In the structures of the native enzyme and of the DNA complex reported previously, the active site of the structure-specific nuclease domain is too far from that of the polymerase domain, making it difficult to propose a structural model for the in vivo primer-excision and nick-translation activities of the enzyme. In the present structure, the two active sites are considerably closer. Taken together, the reported structure of the native enzyme, that of the Fab complex and the present structure imply that the different orientation of the structure-specific nuclease domain is probably a consequence of intrinsically high relative mobility between these two domains in this enzyme.
机译：我由水生栖热菌DNA聚合酶聚合酶,structure-specific核酸酶残留编辑核酸酶域。本机酶的三维结构及其复杂的DNA已经报道。抑制抗体也已确定。原生酶在不同的结构晶体形式报告确定为2.6在这里。测量在钬L(3)边缘价值通过验证的解决方案分子置换。聚合酶域是类似报道以前,的相对取向structure-specific核酸酶域是显著不同于本机酶和DNA复杂;相同结构的观察工厂复杂。酶和DNA的复杂的报道以前,的活性部位structure-specific核酸酶域是太远了从聚合酶的域,使它很难提出的结构模型体内primer-excision nick-translation酶的活动。结构,两个活动网站近了。本机酶,Fab复杂目前的结构意味着不同取向的structure-specific核酸酶域可能是本质上的结果高这两个域之间的相对移动在这种酶。

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