Genomics, evolution, and crystal structure of a new family of bacterial spore kinases.

Genomics, evolution, and crystal structure of a new family of bacterial spore kinases.
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DOI:
10.1002/prot.22663
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发表时间:
2010-05-01
影响因子:
2.9
通讯作者:
Manning, Gerard
Manning, Gerard
中科院分区:
生物学4区
文献类型:
--
作者:
Scheeff, Eric D.;Axelrod, Herbert L.;Miller, Mitchell D.;Chiu, Hsiu-Ju;Deacon, Ashley M.;Wilson, Ian A.;Manning, Gerard

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细菌孢子的形成是一个复杂的过程,与生物学和人类疾病有着根本的关系。孢子外壳结构复杂且知之甚少,许多蛋白质组分的作用仍不清楚。我们描述了一个新的家庭的孢子外壳蛋白,细菌孢子激酶(BSK),和第一个晶体结构的BSK,YtaA(CotI)从枯草芽孢杆菌。BSK广泛分布于芽孢杆菌和梭菌属中,具有动态的进化历史。序列和结构分析表明,BSK是CAK,细菌中普遍存在的一组小分子激酶,与真核蛋白激酶有较远的关系。YtaA与CAK具有实质性的结构相似性,但也显示出独特的特征,拓宽了我们对CAK组的理解。蛋白质表面的进化约束分析表明,BSK家族的成员在底物结合区具有不同的进化枝保守模式,并且可能结合和磷酸化不同的靶标。几类BSKs显然独立地失去了催化活性,成为假激酶,表明该家族也有一个主要的非催化功能。Proteins 2010.© 2009 Wiley-Liss公司。
Bacterial spore formation is a complex process of fundamental relevance to biology and human disease. The spore coat structure is complex and poorly understood, and the roles of many of the protein components remain unclear. We describe a new family of spore coat proteins, the bacterial spore kinases (BSKs), and the first crystal structure of a BSK, YtaA (CotI) from Bacillus subtilis. BSKs are widely distributed in spore-forming Bacillus and Clostridium species, and have a dynamic evolutionary history. Sequence and structure analyses indicate that the BSKs are CAKs, a prevalent group of small molecule kinases in bacteria that is distantly related to the eukaryotic protein kinases. YtaA has substantial structural similarity to CAKs, but also displays distinctive features that broaden our understanding of the CAK group. Evolutionary constraint analysis of the protein surfaces indicates that members of the BSK family have distinct clade-conserved patterns in the substrate binding region, and probably bind and phosphorylate distinct targets. Several classes of BSKs have apparently independently lost catalytic activity to become pseudokinases, indicating that the family also has a major noncatalytic function. Proteins 2010. © 2009 Wiley-Liss, Inc.
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