| Literature DB >> 31891428 |
Yong-Shan Gao1, Yan-Li Wang1, Xiao Wang1, Lin Liu1.
Abstract
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.Entities:
Keywords: zzm321990Synechocystis; AAA+ ring hexamer; ATPase; chlorophyll biosynthesis; magnesium chelatase; motor
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Year: 2020 PMID: 31891428 PMCID: PMC7096714 DOI: 10.1002/pro.3816
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725