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首页> 外文期刊>Biochemistry >Solution Structure of the Endonuclease Domain from the Master Replication Initiator Protein of the Nanovirus Faba Bean Necrotic Yellows Virus and Comparison with the Corresponding Geminivirus and Circovirus Structures
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Solution Structure of the Endonuclease Domain from the Master Replication Initiator Protein of the Nanovirus Faba Bean Necrotic Yellows Virus and Comparison with the Corresponding Geminivirus and Circovirus Structures

机译：从纳米病毒Faba Bean坏死yellows病毒的主核酸酶域的溶液结构来自纳米病毒坏死的蛋白质病毒，与相应的Geminivirus和圆环病毒结构进行比较

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摘要

Nanoviruses are a family of plant viruses that possess a genome of multiple circular single-stranded DNA (ssDNA) components and are strikingly similar in their replication mode to the plant geminiviruses and to the circoviruses that infect birds or mammals. These viruses multiply by rolling circle replication using virus-encoded multifunctional replication initiator proteins (Rep proteins) that catalyze the initiation of replication on a double-stranded DNA (dsDNA) intermediate and the resolution of the ssDNA into circles. Here we report the solution NMR three-dimensional structure of the endonuclease domain from the master Rep (M-Rep) protein of faba bean necrotic yellows virus (FBNYV), a representative of the nanoviruses. The domain comprises amino acids 2-95 (M-Rep_(2-95)), and its global fold is similar to those previously described for the gemini- and circovirus Rep endonuclease domains, consisting of a central 5-stranded antiparallel beta-sheet covered on one side by an alpha-helix and irregular loops and on the other, more open side of the domain, by an alpha-helix containing the catalytic tyrosine residue (the catalytic helix). Longer domain constructs extending to amino acids 117 and 124 were also characterized. They contain an additional alpha-helix, are monomeric, and exhibit catalytic activity indistinguishable from that of M-Rep_(2-95). The binding site for the catalytic metal was identified by paramagnetic broadening and maps to residues on the exposed face of the central beta-sheet. A comparison with the previously determined Rep endonuclease domain structures of tomato yellow leaf curl Sardinia virus (TYLCSV), a geminivirus, and that of porcine circovirus type 2 (PCV2) Rep allows the identification of a positively charged surface that is most likely involved in dsDNA binding, and reveals common features shared by all endonuclease domains of nanovirus, geminivirus, and circovirus Rep proteins.
机译：纳米病毒是一种植物病毒系列，其具有多个圆形单链DNA（SSDNA）组分的基因组，并在其复制模式下令人惊微地相似，以植物的GeminiviRuses和感染鸟类或哺乳动物的循环病毒。这些病毒通过使用病毒编码的多功能复制引发剂蛋白（Rep蛋白）递增圆圈复制，该蛋白质（Rep蛋白）催化在双链DNA（DSDNA）中间体上的复制和SSDNA的分辨率转向圆圈。在这里，我们从Faba Bean坏死的yellows病毒（FBNYV）的主蛋白酶蛋白（M-Rep）蛋白，纳米病毒代表的溶液NMR三维结构。该结构域包含氨基酸2-95（M-REP_（2-95）），其全局折叠类似于先前针对Gemini-和呋喃酚素核酸酶核酸域的那些，包括中央5链的反平行β-片。通过α-螺旋和不规则环覆盖在一侧，并在域的另一个，更开放的侧面，通过含有催化酪氨酸残基（催化螺旋）的α-螺旋。还表征了延伸到氨基酸117和124的更长的结构域构建体。它们含有另外的α-螺旋，是单体，并且表现出与M-REP_（2-95）的催化活性难以区分。通过顺磁性展会和映射到中央β-片的暴露面上的残基的催化金属的结合位点。与先前确定的番茄黄叶卷曲肉毒糖尿病病毒（TylCSv），Geminivirus和猪胃肠病毒2型（PCV2）Rep的比较允许鉴定最可能参与DSDNA的带正电荷的表面结合，并揭示了纳米病毒，Geminivirus和胃肠病毒Rep蛋白的所有内切核酸酶结构域共享的共同特征。

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  • 来源
    《Biochemistry》 |2007年第21期|共12页
  • 作者

    Susana Vega-Rocha; Bruno Gronenborn; Angela M. Gronenborn;

  • 作者单位

    Structural and Computational Biology Program Spanish National Cancer Center (CNIO) Madrid 28029 Spain Institut des Sciences du Vegetal Centre National de la Recherche Scientifique 91198 Gif-sur-Yvette Cedex France Laboratory of Chemical Physi;

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  • 正文语种 eng
  • 中图分类 生物化学;
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