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

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 s...

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Detalles Bibliográficos
Autores principales: Adams, Nathan B. P., Reid, James D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2013
Materias:
Enzymology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3789969/
https://www.ncbi.nlm.nih.gov/pubmed/23940041
http://dx.doi.org/10.1074/jbc.M113.477943
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author Adams, Nathan B. P.
Reid, James D.
author_facet Adams, Nathan B. P.
Reid, James D.
author_sort Adams, Nathan B. P.
collection PubMed
description 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 Mg(2+) and MgATP(2−) binding.
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spelling pubmed-37899692013-10-04 The Allosteric Role of the AAA(+) Domain of ChlD Protein from the Magnesium Chelatase of Synechocystis Species PCC 6803 Adams, Nathan B. P. Reid, James D. J Biol Chem Enzymology 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 Mg(2+) and MgATP(2−) binding. American Society for Biochemistry and Molecular Biology 2013-10-04 2013-08-12 /pmc/articles/PMC3789969/ /pubmed/23940041 http://dx.doi.org/10.1074/jbc.M113.477943 Text en © 2013 by The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice—Final version full access. Creative Commons Attribution Unported License (http://creativecommons.org/licenses/by/3.0/) applies to Author Choice Articles
spellingShingle Enzymology
Adams, Nathan B. P.
Reid, James D.
The Allosteric Role of the AAA(+) Domain of ChlD Protein from the Magnesium Chelatase of Synechocystis Species PCC 6803
title The Allosteric Role of the AAA(+) Domain of ChlD Protein from the Magnesium Chelatase of Synechocystis Species PCC 6803
title_full The Allosteric Role of the AAA(+) Domain of ChlD Protein from the Magnesium Chelatase of Synechocystis Species PCC 6803
title_fullStr The Allosteric Role of the AAA(+) Domain of ChlD Protein from the Magnesium Chelatase of Synechocystis Species PCC 6803
title_full_unstemmed The Allosteric Role of the AAA(+) Domain of ChlD Protein from the Magnesium Chelatase of Synechocystis Species PCC 6803
title_short The Allosteric Role of the AAA(+) Domain of ChlD Protein from the Magnesium Chelatase of Synechocystis Species PCC 6803
title_sort allosteric role of the aaa(+) domain of chld protein from the magnesium chelatase of synechocystis species pcc 6803
topic Enzymology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3789969/
https://www.ncbi.nlm.nih.gov/pubmed/23940041
http://dx.doi.org/10.1074/jbc.M113.477943
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