6fki

Chloroplast F1Fo conformation 3Chloroplast F1Fo conformation 3

6fki, resolution 4.30Å Show:Asymmetric Unit Biological Assembly Structural highlights 6fki is a 26 chain structure with sequence from Spinacia oleracea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 4.3Å Ligands: Experimental data: Check Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ATPI_SPIOL Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Publication Abstract from PubMed The chloroplast adenosine triphosphate (ATP) synthase uses the electrochemical proton gradient generated by photosynthesis to produce ATP, the energy currency of all cells. Protons conducted through the membrane-embedded Fo motor drive ATP synthesis in the F1 head by rotary catalysis. We determined the high-resolution structure of the complete cF1Fo complex by cryo-electron microscopy, resolving side chains of all 26 protein subunits, the five nucleotides in the F1 head, and the proton pathway to and from the rotor ring. The flexible peripheral stalk redistributes differences in torsional energy across three unequal steps in the rotation cycle. Plant ATP synthase is autoinhibited by a beta-hairpin redox switch in subunit gamma that blocks rotation in the dark. Structure, mechanism, and regulation of the chloroplast ATP synthase.,Hahn A, Vonck J, Mills DJ, Meier T, Kuhlbrandt W Science. 2018 May 11;360(6389). pii: 360/6389/eaat4318. doi:, 10.1126/science.aat4318. PMID:29748256 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATPase 3D structures