7l1q | pdb_00007l1q

PS3 F1-ATPase Binding/TS Dwell

spinqualitylabelsall models 7l1q, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7l1q is a 7 chain structure with sequence from Bacillus sp. PS3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.4Å Ligands: ADP, ATP, MG, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0M3VGF9_BACP3 Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.[HAMAP-Rule:MF_01346] Publication Abstract from PubMed F(1)F(o) ATP synthase interchanges phosphate transfer energy and proton motive force via a rotary catalysis mechanism. Isolated F(1)-ATPase catalytic cores can hydrolyze ATP, passing through six intermediate conformational states to generate rotation of their central gamma-subunit. Although previous structural studies have contributed greatly to understanding rotary catalysis in the F(1)-ATPase, the structure of an important conformational state (the binding-dwell) has remained elusive. Here, we exploit temperature and time-resolved cryo-electron microscopy to determine the structure of the binding- and catalytic-dwell states of Bacillus PS3 F(1)-ATPase. Each state shows three catalytic beta-subunits in different conformations, establishing the complete set of six states taken up during the catalytic cycle and providing molecular details for both the ATP binding and hydrolysis strokes. We also identify a potential phosphate-release tunnel that indicates how ADP and phosphate binding are coordinated during synthesis. Overall these findings provide a structural basis for the entire F(1)-ATPase catalytic cycle. , PMID:34344897 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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