Crystal structure of FtsA from Staphylococcus aureus

被引：30

作者：

Fujita, Junso ^{[1
]}

Maeda, Yoko ^{[1
]}

Nagao, Chioko ^{[3
]}

Tsuchiya, Yuko ^{[3
]}

Miyazaki, Yuma ^{[1
]}

Hirose, Mika ^{[2
]}

Mizohata, Eiichi ^{[1
]}

Matsumoto, Yoshimi ^{[4
]}

Inoue, Tsuyoshi ^{[1
]}

Mizuguchi, Kenji ^{[3
]}

Matsumura, Hiroyoshi ^{[1
]}

机构：

[1] Osaka Univ, Grad Sch Engn, Dept Appl Chem, Suita, Osaka 5650871, Japan

[2] Osaka Univ, Grad Sch Sci, Dept Chem, Toyonaka, Osaka 5600043, Japan

[3] Natl Inst Biomed Innovat, Ibaraki, Osaka 5670085, Japan

[4] Osaka Univ, Inst Sci & Ind Res, Lab Microbiol & Infect Dis, Ibaraki, Osaka 5670047, Japan

来源：

FEBS LETTERS | 2014年 / 588卷 / 10期

基金：

日本学术振兴会;

关键词：

Bacterial divisome; Staphylococcus aureus; FtsA; FtsZ; CELL-DIVISION PROTEIN; BACTERIAL CYTOKINESIS; Z-RING; ACTIN; CYTOSKELETON; MEMBRANE; SEQUENCE;

D O I：

10.1016/j.febslet.2014.04.008

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The bacterial cell-division protein FtsA anchors FtsZ to the cytoplasmic membrane. But how FtsA and FtsZ interact during membrane division remains obscure. We have solved 2.2 angstrom resolution crystal structure for FtsA from Staphylococcus aureus. In the crystals, SaFtsA molecules within the dimer units are twisted, in contrast to the straight filament of FtsA from Thermotoga maritima, and the half of S12-S13 hairpin regions are disordered. We confirmed that SaFtsZ and SaFtsA associate in vitro, and found that SaFtsZ GTPase activity is enhanced by interaction with SaFtsA. Structured summary of protein interactions: SaFtsA and SaFtsZ bind by comigration in non denaturing gel electrophoresis (View interaction) SaFtsZ and SaFtsA bind by molecular sieving (View interaction) SaFtsA and SaFtsA bind by x-ray crystallography (View interaction) (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：1879 / 1885

页数：7

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