5y5y

V/A-type ATPase/synthase from Thermus thermophilus, peripheral domain, rotational state 1V/A-type ATPase/synthase from Thermus thermophilus, peripheral domain, rotational state 1

5y5y, resolution 4.70Å Show:Asymmetric Unit Biological Assembly Structural highlights 5y5y is a 13 chain structure with sequence from Thermus thermophilus hb8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Activity: H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Experimental data: Check Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [VATE_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. [VATF_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. [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. [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. Publication Abstract from PubMed Proton translocating rotary ATPases couple ATP hydrolysis/synthesis, which occurs in the soluble domain, with proton flow through the membrane domain via a rotation of the common central rotor complex against the surrounding peripheral stator apparatus. Here, we present a large data set of single particle cryo-electron micrograph images of the V/A type H(+)-rotary ATPase from the bacterium Thermus thermophilus, enabling the identification of three rotational states based on the orientation of the rotor subunit. Using masked refinement and classification with signal subtractions, we obtain homogeneous reconstructions for the whole complexes and soluble V1 domains. These reconstructions are of higher resolution than any EM map of intact rotary ATPase reported previously, providing a detailed molecular basis for how the rotary ATPase maintains structural integrity of the peripheral stator apparatus, and confirming the existence of a clear proton translocation path from both sides of the membrane. Cryo EM structure of intact rotary H(+)-ATPase/synthase from Thermus thermophilus.,Nakanishi A, Kishikawa JI, Tamakoshi M, Mitsuoka K, Yokoyama K Nat Commun. 2018 Jan 8;9(1):89. doi: 10.1038/s41467-017-02553-6. PMID:29311594 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATPase 3D structures