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Publication Abstract from PubMed

Magnesium chelatase (MgCh) is a heterotrimeric enzyme complex, composed of two AAA+ family subunits that can assembly into a double ring structure and a large catalytic subunit. The small AAA+ subunit has ATPase activity and can self-oligomerize into a ring structure, while the other AAA+ subunit lacks independent ATPase activity. Previous structural studies of the ATPase motor subunit of MgCh from a bacteriochlorophyll-synthesizing bacterium have identified a unique ATPase clade, but the model of oligomeric assembly is unclear. Here we present the hexameric structure of the MgCh ATPase motor subunit from the chlorophyll-synthesizing cyanobacterium Synechocystis sp. PCC 6803. This structure reveals details of how the hexameric ring is assembled, and thus provides a basis for further studying the heterotrimeric complex.

Hexameric structure of the ATPase motor subunit of magnesium chelatase in chlorophyll biosynthesis.,Gao YS, Wang YL, Wang X, Liu L Protein Sci. 2020 Apr;29(4):1040-1046. doi: 10.1002/pro.3816. Epub 2020 Jan 7. PMID:31891428^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.