ArticleThe Journal of biological chemistry2013
The allosteric role of the AAA+ domain of ChlD protein from the magnesium chelatase of synechocystis species PCC 6803.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- The structural chemistry and biosynthesis of chlorophylls.RSC chemical biology · 2026Review
- Commensal gut bacteria employ de-chelatase HmuS to harvest iron from heme.The EMBO journal · 2025Article
- Regulatory and retrograde signaling networks in the chlorophyll biosynthetic pathway.Journal of integrative plant biology · 2025Review
- Mutagenesis selection and large-scale cultivation of non-greenFrontiers in nutrition · 2024Article
- Absolute quantification of cellular levels of photosynthesis-related proteins in Synechocystis sp. PCC 6803.Photosynthesis research · 2023Article
- The active site of magnesium chelatase.Nature plants · 2020Article
- Hexameric structure of the ATPase motor subunit of magnesium chelatase in chlorophyll biosynthesis.Protein science : a publication of the Protein Society · 2020Article
- The ChlD subunit links the motor and porphyrin binding subunits of magnesium chelatase.The Biochemical journal · 2019Article
- Phosphorylation of GENOMES UNCOUPLED 4 Alters Stimulation of Mg Chelatase Activity in Angiosperms.Plant physiology · 2016Article
- Article
- Nanomechanical and Thermophoretic Analyses of the Nucleotide-Dependent Interactions between the AAA(+) Subunits of Magnesium Chelatase.Journal of the American Chemical Society · 2016Article
- The Crystal Structure of the Ubiquitin-like Domain of Ribosome Assembly Factor Ytm1 and Characterization of Its Interaction with the AAA-ATPase Midasin.The Journal of biological chemistry · 2016Article
- Structural and functional consequences of removing the N-terminal domain from the magnesium chelatase ChlH subunit of Thermosynechococcus elongatus.The Biochemical journal · 2014Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
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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Registered trials
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