22vl

Cryo-EM structure of Chlamydomonas reinhardtii chloroplast F1Fo-ATP synthase

spinqualitylabelsall models 22vl, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 22vl is a 26 chain structure with sequence from Chlamydomonas reinhardtii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.2Å Ligands: ATP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ATPI_CHLRE F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Publication Abstract from PubMed F(1)F(o)-ATP synthase is a multi-subunit energy-producing macromolecular machine, consisting of hydrophilic F(1) and hydrophobic F(o) segments, which utilize transmembrane electrochemical potential to synthesize ATP from ADP and inorganic phosphate. ATP synthases are widely distributed in the inner membrane of mitochondria, the thylakoid membrane of chloroplasts, and the plasma membrane of bacteria. To date, a comprehensively structural study on chloroplast F(1)F(o)-ATP synthase is very limited compared with their counterparts in mitochondria and bacteria. In this study, we in-situ extracted and purified chloroplast F(1)F(o)-ATP synthase from the photosynthetic unicellular green algae Chlamydomonas reinhardtii. The ATPase activity of the holoenzyme was validated by a combination of BN-PAGE separation and in-gel detection. We determined the structure of Chlamydomonas reinhardtii F(1)F(o)-ATP synthase at 3.2 A resolution using single particle cryo-electron microscopy (cryo-EM). The structure is in an oxidized state with a disulfide bond formation in the gamma subunit. More acidic residues were found to be involved in the proton translocation across the F(o) segment compared with their counterparts of the higher plants. Overall, the structure presented here provides novel structural information, giving us comprehensive understanding of the photosynthetic chloroplast F(1)F(o)-ATP synthase from lower unicellular algae to higher plants. Cryo-EM structure of Chlamydomonas reinhardtii chloroplast F(1)F(o)-ATP synthase.,Liu J, Li D, Wang Q, Yin P, Guan Z, Yan J Biochem Biophys Res Commun. 2026 Apr 30;811:153552. doi: , 10.1016/j.bbrc.2026.153552. Epub 2026 Mar 2. PMID:41819751 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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