6r10 | pdb_00006r10

Thermus thermophilus V/A-type ATPase/synthase, rotational state 1R

Loading... Status: waiting for Mol* initialization Structural highlights 6r10 is a 26 chain structure with sequence from Thet8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, MG Related: 6qum, 6r0w, 6r0z, 6r0y Activity: H(+)-transporting two-sector ATPase, with EC number 7.1.2.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [VATE_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. [VATD_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. [VATC_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. [VATB_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type beta chain is a regulatory subunit. [VATA_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type alpha chain is a catalytic subunit. [VATF_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. Publication Abstract from PubMed V (vacuolar)/A (archaeal)-type adenosine triphosphatases (ATPases), found in archaea and eubacteria, couple ATP hydrolysis or synthesis to proton translocation across the plasma membrane using the rotary-catalysis mechanism. They belong to the V-type ATPase family, which differs from the mitochondrial/chloroplast F-type ATP synthases in overall architecture. We solved cryo-electron microscopy structures of the intact Thermus thermophilus V/A-ATPase, reconstituted into lipid nanodiscs, in three rotational states and two substates. These structures indicate substantial flexibility between V1 and Vo in a working enzyme, which results from mechanical competition between central shaft rotation and resistance from the peripheral stalks. We also describe details of adenosine diphosphate inhibition release, V1-Vo torque transmission, and proton translocation, which are relevant for the entire V-type ATPase family. Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase.,Zhou L, Sazanov LA Science. 2019 Aug 23;365(6455). pii: 365/6455/eaaw9144. doi:, 10.1126/science.aaw9144. PMID:31439765 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATPase 3D structures

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