6n2d

Bacillus PS3 ATP synthase membrane regionBacillus PS3 ATP synthase membrane region

6n2d, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Structural highlights 6n2d is a 13 chain structure with sequence from Bacp3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 6n2y, 6n2z, 6n30 Gene: atpF (BACP3), atpB (BACP3), atpE, uncE (BACP3) Experimental data: Check Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ATPL_BACP3] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.[HAMAP-Rule:MF_01396] Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of 10 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.[HAMAP-Rule:MF_01396] Publication Abstract from PubMed ATP synthases produce ATP from ADP and inorganic phosphate with energy from a transmembrane proton motive force. Bacterial ATP synthases have been studied extensively because they are the simplest form of the enzyme and because of the relative ease of genetic manipulation of these complexes. We expressed the Bacillus PS3 ATP synthase in Eschericia coli, purified it, and imaged it by cryo-EM, allowing us to build atomic models of the complex in three rotational states. The position of subunit epsilon shows how it is able to inhibit ATP hydrolysis while allowing ATP synthesis. The architecture of the membrane region shows how the simple bacterial ATP synthase is able to perform the same core functions as the equivalent, but more complicated, mitochondrial complex. The structures reveal the path of transmembrane proton translocation and provide a model for understanding decades of biochemical analysis interrogating the roles of specific residues in the enzyme. Structure of a bacterial ATP synthase.,Guo H, Suzuki T, Rubinstein JL Elife. 2019 Feb 6;8. pii: 43128. doi: 10.7554/eLife.43128. PMID:30724163 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.