大肠杆菌HspQ的X射线晶体结构，一种参与延缓复制起始的蛋白质。

X-ray crystal structure of Escherichia coli HspQ, a protein involved in the retardation of replication initiation.

作者信息

Abe Yoshito, Shioi Seijiro, Kita Shunsuke, Nakata Hikaru, Maenaka Katsumi, Kohda Daisuke, Katayama Tsutomu, Ueda Tadashi

机构信息

Department of Protein Structure, Function and Design, Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka, Japan.

Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.

出版信息

FEBS Lett. 2017 Nov;591(22):3805-3816. doi: 10.1002/1873-3468.12892. Epub 2017 Nov 12.

DOI:10.1002/1873-3468.12892

PMID:29083032

Abstract

The heat shock protein HspQ (YccV) of Escherichia coli has been proposed to participate in the retardation of replication initiation in cells with the dnaA508 allele. In this study, we have determined the 2.5-Å-resolution X-ray structure of the trimer of HspQ, which is also the first structure of a member of the YccV superfamily. The acidic character of the HspQ trimer suggests an interaction surface with basic proteins. From these results, we discuss the cellular function of HspQ, including its relationship with the DnaA508 protein.

摘要

大肠杆菌的热休克蛋白HspQ（YccV）被认为参与了具有dnaA508等位基因的细胞中复制起始的延迟。在本研究中，我们确定了HspQ三聚体的2.5埃分辨率X射线结构，这也是YccV超家族成员的首个结构。HspQ三聚体的酸性特征表明其与碱性蛋白存在相互作用表面。基于这些结果，我们讨论了HspQ的细胞功能，包括其与DnaA508蛋白的关系。