AN ATPASE DOMAIN COMMON TO PROKARYOTIC CELL-CYCLE PROTEINS, SUGAR KINASES, ACTIN, AND HSP70 HEAT-SHOCK PROTEINS

AN ATPASE DOMAIN COMMON TO PROKARYOTIC CELL-CYCLE PROTEINS, SUGAR KINASES, ACTIN, AND HSP70 HEAT-SHOCK PROTEINS
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DOI:
10.1073/pnas.89.16.7290
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发表时间:
1992-08-15
影响因子:
11.1
通讯作者:
VALENCIA, A
VALENCIA, A
中科院分区:
综合性期刊1区
文献类型:
--
作者:
BORK, P;SANDER, C;VALENCIA, A

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功能多样的肌动蛋白、己糖激酶和hsp70蛋白家族共同具有已知三维结构的ATP酶结构域。优化叠加的三个结构和在每个三个家庭中的许多序列的比对揭示了一组共同的保守残基,分布在五个序列基序,这是参与ATP结合,并在一个假定的域间铰链。根据这些基序中的多序列比对,定义了每个位置所需的氨基酸性质的模式。该模式的区分能力部分是由于使用了几种已知的三维结构和许多序列,部分是由于从观察到的氨基酸频率概括到每个序列位置处的氨基酸适合度的“性质”方法。序列数据库搜索与模式显著匹配的糖激酶,如岩藻糖激酶,木糖激酶,核糖激酶和甘油激酶,以及原核细胞周期蛋白MreB,FtsA和StbA。这些被预测为具有与己糖激酶、肌动蛋白和Hsc 70的ATP酶亚结构域Ia和IIa相同的三级结构的亚结构域,非常相似的ATP结合口袋,以及伴随功能状态变化的结构域间铰链运动的能力。一个共同的进化起源的所有蛋白质在这一类的建议。
The functionally diverse actin, hexokinase, and hsp70 protein families have in common an ATPase domain of known three-dimensional structure. Optimal superposition of the three structures and alignment of many sequences in each of the three families has revealed a set of common conserved residues, distributed in five sequence motifs, which are involved in ATP binding and in a putative interdomain hinge. From the multiple sequence alignment in these motifs a pattern of amino acid properties required at each position is defined. The discriminatory power of the pattern is in part due to the use of several known three-dimensional structures and many sequences and in part to the "property" method of generalizing from observed amino acid frequencies to amino acid fitness at each sequence position. A sequence data base search with the pattern significantly matches sugar kinases, such as fuco-, glucono-, xylulo-, ribulo-, and glycerokinase, as well as the prokaryotic cell cycle proteins MreB, FtsA, and StbA. These are predicted to have subdomains with the same tertiary structure as the ATPase subdomains Ia and IIa of hexokinase, actin, and Hsc70, a very similar ATP binding pocket, and the capacity for interdomain hinge motion accompanying functional state changes. A common evolutionary origin for all of the proteins in this class is proposed.