Structural basis of severe acute respiratory syndrome coronavirus ADP-ribose-1''-phosphate dephosphorylation by a conserved domain of nsP3.
Structural basis of severe acute respiratory syndrome coronavirus ADP-ribose-1''-phosphate dephosphorylation by a conserved domain of nsP3.
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DOI：
10.1016/j.str.2005.07.022
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发表时间：
2005-11
期刊：
影响因子：
--
通讯作者：
Kuhn P
中科院分区：
文献类型：
--
作者：
Saikatendu KS;Joseph JS;Subramanian V;Clayton T;Griffith M;Moy K;Velasquez J;Neuman BW;Buchmeier MJ;Stevens RC;Kuhn P
严重急性呼吸综合征冠状病毒 (SARS-CoV) 非结构蛋白 3 (nsP3) 保守结构域的晶体结构已通过单波长异常色散解析至 1.4 Å 分辨率。这种“X”结构域的结构在许多单链 RNA 病毒中都可见，揭示了一个三层的 α/β/α 核心，具有类似大 H2A 的折叠。假定的活性位点是一个暴露于溶剂的裂口，在其三种结构同源物（酵母 Ymx7、Archeoglobus fulgidus AF1521 和来自大肠杆菌的 Er58）中是保守的。其序列与酵母 YBR022W（也称为 Poa1P）相似，后者是一种作用于 ADP-核糖-1″-磷酸 (Appr-1″-p) 的已知磷酸酶。在体外试验中，SARS nsP3 结构域很容易从 Appr-1"-p 中去除 1" 磷酸基团，证实了其磷酸酶活性。所有已知宏 H2A 结构域的序列和结构比较以及可用的功能数据表明，该超家族的蛋白质形成了一组新兴的核苷酸磷酸酶，可将 Appr-1"-p 去磷酸化。
The crystal structure of a conserved domain of nonstructural protein 3 (nsP3) from severe acute respiratory syndrome coronavirus (SARS-CoV) has been solved by single-wavelength anomalous dispersion to 1.4 Å resolution. The structure of this “X” domain, seen in many single-stranded RNA viruses, reveals a three-layered α/β/α core with a macro-H2A-like fold. The putative active site is a solvent-exposed cleft that is conserved in its three structural homologs, yeast Ymx7, Archeoglobus fulgidus AF1521, and Er58 from E. coli. Its sequence is similar to yeast YBR022W (also known as Poa1P), a known phosphatase that acts on ADP-ribose-1″-phosphate (Appr-1″-p). The SARS nsP3 domain readily removes the 1″ phosphate group from Appr-1″-p in in vitro assays, confirming its phosphatase activity. Sequence and structure comparison of all known macro-H2A domains combined with available functional data suggests that proteins of this superfamily form an emerging group of nucleotide phosphatases that dephosphorylate Appr-1″-p.
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影响因子：
56.9
作者：
CULVER, GM;MCCRAITH, SM;PHIZICKY, EM
通讯作者：
PHIZICKY, EM
影响因子：
3.7
作者：
Lanciotti, RS;Ludwig, ML;Miller, BR
通讯作者：
Miller, BR
影响因子：
5.6
作者：
CHARLIER, D;HASSANZADEH, G;GLANSDORFF, N
通讯作者：
GLANSDORFF, N
影响因子：
4.8
作者：
Gioia, U;Laneve, P;Caffarelli, E
通讯作者：
Caffarelli, E
DOI：
10.1107/s0907444994003112
发表时间：
1994-09-01
期刊：
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子：
--
作者：
BAILEY, S
通讯作者：
BAILEY, S