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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >CRYSTAL STRUCTURE OF THE CELL CYCLE-REGULATORY PROTEIN SUC1 REVEALS A BETA-HINGE CONFORMATIONAL SWITCH
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CRYSTAL STRUCTURE OF THE CELL CYCLE-REGULATORY PROTEIN SUC1 REVEALS A BETA-HINGE CONFORMATIONAL SWITCH

机译：细胞周期调节蛋白SUC1的晶体结构揭示了β-铰链构象开关

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摘要

The Schizosaccharomyces pombe cell cycle-regulatory protein suc1, named as the suppressor of cdc2 temperature-sensitive mutations, is essential for cell cycle progression. To understand suc1 structure-function relationships and to help resolve conflicting interpretations of suc1 function based on genetic studies of suc1 and its functional homologs in both lower and higher eukaryotes, we have determined the crystal structure of the beta-interchanged suc1 dimer, Each domain consists of three alpha-helices and a four-stranded beta-sheet, completed by the interchange of terminal beta-strands between the two subunits, This beta-interchanged suc1 dimer, when compared with the beta-hairpin single-domain folds of suc1, reveals a beta-hinge motif formed by the conserved amino acid sequence HVPEPH. This beta-hinge mediates the subunit conformation and assembly of suc1: closing produces the intrasubunit beta-hairpin and single-domain fold, whereas opening leads to the intersubunit beta-strand interchange and interlocked dimer assembly reported here, This conformational switch markedly changes the surface accessibility of sequence-conserved residues available for recognition of cyclin-dependent kinase, suggesting a structural mechanism for beta-hinge-mediated regulation of suc1 biological function. Thus, suc1 belongs to the family of domain-swapping proteins, consisting of intertwined and dimeric protein structures in which the dual assembly modes regulate their function. [References: 33]
机译：粟酒裂殖酵母细胞周期调节蛋白suc1，被称为cdc2温度敏感突变的抑制子，对细胞周期进程至关重要。为了了解suc1结构与功能之间的关系，并根据对suc1及其功能同源物在低等和高等真核生物中的遗传研究，帮助解决suc1功能的矛盾解释，我们确定了β互换suc1二聚体的晶体结构。通过两个亚基之间末端β链的互换完成的三个α-螺旋和四链β-折叠的折叠，与suc1的β-发夹单结构域折叠相比，该β互换的suc1二聚体显示由保守的氨基酸序列HVPEPH形成的β铰链基序。此β-铰链介导suc1的亚基构象和组装：闭合产生亚基内β-发夹和单域折叠，而打开导致此处报道的亚基间β-链互换和互锁的二聚体组装，这种构象开关显着改变了表面可用于识别细胞周期蛋白依赖性激酶的序列保守残基的可及性，提示了β-铰链介导的suc1生物学功能调节的结构机制。因此，suc1属于结构域交换蛋白家族，由相互缠绕和二聚的蛋白质结构组成，其中双重组装模式调节其功能。 [参考：33]

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