I型β旋转在五肽重复蛋白中产生新的扭曲:Nostoc sp. PCC 7120的Alr5209的晶体结构在1.7 angström分辨率下测定

IF 3.5 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY
Ruojing Zhang, Shuisong Ni, Michael A. Kennedy
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引用次数: 4

摘要

五肽重复蛋白(PRPs)在蓝藻中大量存在,在一些基因组中有几十个,例如在Nostoc sp. PCC 7120中。PRPs由五个氨基酸的重复一致序列组成,采用独特的右手四边形β-螺旋结构,也称为重复五残基(Rfr)折叠,由四个连续的五肽重复形成的线圈堆叠而成。右旋四边形β-螺旋PRP结构是通过在给定线圈的四个角上重复β旋转来构建的,每个角都导致多肽链方向发生90°变化。到目前为止,所有PRP结构都由II型和IV型β转变或完全由II型β转变组成。在这里,我们报道了由I型和II型β匝组成的PRP的第一个结构,Alr5209来自Nostoc sp. PCC 7120。alr5209基因编码129个氨基酸,包含16个串联五肽重复序列。将Alr5209结构与所有其他PRPs进行比较,以确定I型β转如何被容纳在Rfr折叠中,以及I型β转对右手四边形β-螺旋结构的影响。考虑到Alr5209代表了第一个包含I型β匝数的PRP结构,我们对PRP共识序列进行了重新评估和更新。尽管对PRP结构的研究越来越多,但它们的功能在很大程度上仍然未知。基因组分析表明,alr5209位于一个五基因操纵子(alr5208-alr5212)中,Alr5211被注释为NADH脱氢酶,表明alr5209可能参与氧化磷酸化。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Type I beta turns make a new twist in pentapeptide repeat proteins: Crystal structure of Alr5209 from Nostoc sp. PCC 7120 determined at 1.7 angström resolution

Type I beta turns make a new twist in pentapeptide repeat proteins: Crystal structure of Alr5209 from Nostoc sp. PCC 7120 determined at 1.7 angström resolution

Pentapeptide repeat proteins (PRPs) are found abundantly in cyanobacteria, numbering in the dozens in some genomes, e.g. in Nostoc sp. PCC 7120. PRPs, comprised of a repeating consensus sequence of five amino acids, adopt a distinctive right-handed quadrilateral β-helical structure, also referred to as a repeat five residue (Rfr) fold, made up of stacks of coils formed by four consecutive pentapeptide repeats. The right-handed quadrilateral β-helical PRP structure is constructed by repeating β turns at each of four corners in a given coil, each causing a 90° change in direction of the polypeptide chain. Until now, all PRP structures have consisted either of type II and IV β turns or exclusively of type II β turns. Here, we report the first structure of a PRP comprised of type I and II β turns, Alr5209 from Nostoc sp. PCC 7120. The alr5209 gene encodes 129 amino acids containing 16 tandem pentapeptide repeats. The Alr5209 structure was analyzed in comparison to all other PRPs to determine how type I β turns can be accommodated in Rfr folds and the consequences of type I β turns on the right-handed quadrilateral β-helical structure. Given that Alr5209 represents the first PRP structure containing type I β turns, the PRP consensus sequence was reevaluated and updated. Despite a growing number of PRP structural investigations, their function remains largely unknown. Genome analysis indicated that alr5209 resides in a five-gene operon (alr5208-alr5212) with Alr5211 annotated to be a NADH dehydrogenase indicating Alr5209 may be involved in oxidative phosphorylation.

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来源期刊
Journal of Structural Biology: X
Journal of Structural Biology: X Biochemistry, Genetics and Molecular Biology-Structural Biology
CiteScore
6.50
自引率
0.00%
发文量
20
审稿时长
62 days
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