5zzn
From Proteopedia
Crystal structure of photosystem II from an SQDG-deficient mutant of Thermosynechococcus elongatus
Structural highlights
FunctionPSBA1_THEVB Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.[HAMAP-Rule:MF_01379][1] [2] [3] Publication Abstract from PubMedSulfoquinovosyl-diacylglycerol (SQDG) is one of the four lipids present in the thylakoid membranes. Depletion of SQDG causes different degrees of effects on photosynthetic growth and activities in different organisms. Four SQDG molecules bind to each monomer of the photosystem II (PSII), but their role in PSII function has not been characterized in detail, and no PSII structure without SQDG has been reported. We analyzed the activities of PSII from an SQDG-deficient mutant of the cyanobacterium Thermosynechococcus elongatus by various spectroscopic methods, which showed that depletion of SQDG partially impaired the PSII activity by impairing secondary quinone (QB) exchange at the acceptor site. We further solved the crystal structure of the PSII dimer from the SQDG deletion mutant at 2.1 A resolution, and found that all of the four SQDG-binding sites were occupied by other lipids, most likely PG molecules. Replacement of SQDG at a site near the head of QB provides a possible explanation for the QB impairment. The replacement of two SQDGs located at the monomer-monomer interface by other lipids decreased the stability of PSII dimer, resulting in an increase in the amount of PSII monomer in the mutant. The present results thus suggest that while SQDG binding in all of the PSII biding sites is necessary to fully maintain the activity and stability of PSII, replacement of SQDG by other lipids can partially compensate for their functions. Thylakoid membrane lipid sulfoquinovosyl-diacylglycerol (SQDG) is required for full functioning of photosystem II in Thermosynechococcus elongatus.,Nakajima Y, Umena Y, Nagao R, Endo K, Kobayashi K, Akita F, Suga M, Wada H, Noguchi T, Shen JR J Biol Chem. 2018 Aug 3. pii: RA118.004304. doi: 10.1074/jbc.RA118.004304. PMID:30076221[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Large Structures | Thermosynechococcus vestitus BP-1 | Akita F | Endo K | Kobayashi K | Nagao R | Nakajima Y | Noguchi T | Shen JR | Suga M | Umena Y | Wada H
