6L8D

Hexameric structure of the ATPase subunit of magnesium chelatase

Summary for 6L8D

• Entry DOI: 10.2210/pdb6l8d/pdb
• Descriptor: Magnesium-chelatase subunit ChlI (2 entities in total)
• Functional Keywords: aaa+, atpase, magnesium chelatase, chlorophyll biosynthesis, hydrolase
• Biological source: Synechocystis sp. PCC 6803 substr. Kazusa
• Total number of polymer chains: 6
• Total formula weight: 243499.52

Authors

Gao, Y.,Liu, L. (deposition date: 2019-11-05, release date: 2020-01-15, Last modification date: 2023-11-22)

Primary citation

Gao, Y.S.,Wang, Y.L.,Wang, X.,Liu, L.
Hexameric structure of the ATPase motor subunit of magnesium chelatase in chlorophyll biosynthesis.
Protein Sci., 29:1040-1046, 2020

PubMed 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.

PubMed: 31891428
DOI: 10.1002/pro.3816

Experimental method

X-RAY DIFFRACTION (2.91 Å)