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
Descripción
Sumario: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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