5tsj | pdb_00005tsj

Thermus thermophilus V/A-ATPase bound to VH dAbs

spinqualitylabelsall models 5tsj, resolution 8.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5tsj is a 28 chain structure with sequence from Human and Thet8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Activity: H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [VATF_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. [VATE_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_THET2] 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. [VATD_THET2] Produces ATP from ADP in the presence of a proton gradient across the membrane. Publication Abstract from PubMed The bacterial A/V-type ATPase/synthase rotary motor couples ATP hydrolysis/synthesis with proton translocation across biological membranes. The A/V-type ATPase/synthase from Thermus thermophilus has been extensively studied both structurally and functionally for many years. Here we provide an 8.7A resolution cryo-electron microscopy 3D reconstruction of this complex bound to single-domain antibody fragments, small monomeric antibodies containing just the variable heavy domain. Docking of known structures into the density revealed the molecular orientation of the domain antibodies, suggesting that structure determination of co-domain antibody:protein complexes could be a useful avenue for unstable or smaller proteins. Although previous studies suggested that the presence of fluoroaluminate in this complex could change the rotary state of this enzyme, we observed no gross structural rearrangements under these conditions. Cryo-EM analysis of a domain antibody bound rotary ATPase complex.,Davies RB, Smits C, Wong AS, Stock D, Christie M, Sandin S, Stewart AG J Struct Biol. 2017 Jan 20. pii: S1047-8477(17)30013-8. doi:, 10.1016/j.jsb.2017.01.002. PMID:28115258 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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