The Allosteric Role of the AAA+ Domain of ChlD Protein from the Magnesium Chelatase of Synechocystis Species PCC 6803

被引：20

作者：

Adams, Nathan B. P. ^{[1
]}

Reid, James D. ^{[1
]}

机构：

[1] Univ Sheffield, Dept Chem, Sheffield S3 7HF, S Yorkshire, England

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2013年 / 288卷 / 40期

基金：

英国生物技术与生命科学研究理事会;

关键词：

ATPases; Biosynthesis; Enzyme Catalysis; Mutagenesis Site-specific; Porphyrin; PROTOPORPHYRIN IX CHELATASE; ATPASE ACTIVITY; RHODOBACTER-SPHAEROIDES; ESCHERICHIA-COLI; BARLEY MUTANTS; MG-CHELATASE; SUBUNIT; PCC6803; HYDROLYSIS; COMPLEX;

D O I：

10.1074/jbc.M113.477943

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：

Magnesium chelatase is an AAA(+) ATPase that catalyzes the first step in chlorophyll biosynthesis, the energetically unfavorable insertion of a magnesium ion into a porphyrin ring. This enzyme contains two AAA(+) domains, one active in the ChlI protein and one inactive in the ChlD protein. Using a series of mutants in the AAA(+) domain of ChlD, we show that this site is essential for magnesium chelation and allosterically regulates Mg2+ and MgATP(2-) binding.

引用

页码：28727 / 28732

页数：6

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