6l8d | pdb_00006l8d

Hexameric structure of the ATPase subunit of magnesium chelatase

spinqualitylabelsall models 6l8d, resolution 2.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6l8d is a 6 chain structure with sequence from Syny3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: chlI, slr1030 (SYNY3) Activity: Magnesium chelatase, with EC number 6.6.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CHLI_SYNY3] Involved in chlorophyll biosynthesis; introduces a magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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