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来自 ragged hills 纺锤形病毒的 D212 晶体结构揭示了 PD-(D/E)XK 核酸酶超家族的一个新成员。

The crystal structure of D212 from sulfolobus spindle-shaped virus ragged hills reveals a new member of the PD-(D/E)XK nuclease superfamily.

机构信息

Thermal Biology Institute, Montana State University, Bozeman, MT 59717, USA.

出版信息

J Virol. 2010 Jun;84(12):5890-7. doi: 10.1128/JVI.01663-09. Epub 2010 Apr 7.

DOI:10.1128/JVI.01663-09
PMID:20375162
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2876643/
Abstract

Structural studies have made significant contributions to our understanding of Sulfolobus spindle-shaped viruses (Fuselloviridae), an important model system for archaeal viruses. Continuing these efforts, we report the structure of D212 from Sulfolobus spindle-shaped virus Ragged Hills. The overall fold and conservation of active site residues place D212 in the PD-(D/E)XK nuclease superfamily. The greatest structural similarity is found to the archaeal Holliday junction cleavage enzymes, strongly suggesting a role in DNA replication, repair, or recombination. Other roles associated with nuclease activity are also considered.

摘要

结构研究为我们理解硫矿螺旋状噬菌体（Fuselloviridae）做出了重大贡献，而后者是研究古菌病毒的重要模型系统。为了延续这些努力，我们报道了 Ragged Hills 硫矿螺旋状噬菌体 D212 的结构。其整体折叠和活性位点残基的保守性表明 D212 属于 PD-(D/E)XK 核酸内切酶超家族。与古菌 Holliday 连接酶的结构最为相似，强烈提示其在 DNA 复制、修复或重组中发挥作用。此外，我们还考虑了与核酸内切酶活性相关的其他作用。