Solution structure of SpoIIAA, a phosphorylatable component of the system that regulates transcription factor σF of Bacillus subtilis

被引：54

作者：

Kovacs, H ^{[1
]}

Comfort, D ^{[1
]}

Lord, M ^{[1
]}

Campbell, ID ^{[1
]}

Yudkin, MD ^{[1
]}

机构：

[1] Univ Oxford, Dept Biochem, Microbiol Unit, Oxford OX1 3QU, England

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1998年 / 95卷 / 09期

基金：

英国惠康基金;

关键词：

D O I：

10.1073/pnas.95.9.5067

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The establishment of differential gene expression in sporulating Bacillus subtilis involves four protein components, one of which, SpoIIAA, undergoes phosphorylation and dephosphorylation, We have used NMR spectroscopy to determine the solution structure of the nonphosphorylated form of SpoIIAA, The structure shows a fold consisting of a four-stranded beta-sheet and four alpha-helices. Knowledge of the structure helps to account for the phenotype of several strains of B. subtilis that carry known spoIIAA mutations and should facilitate investigations of the conformational consequences of phosphorylation.

引用

页码：5067 / 5071

页数：5

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