2XND

Crystal structure of bovine F1-c8 sub-complex of ATP Synthase

Summary for 2XND

• Entry DOI: 10.2210/pdb2xnd/pdb
• Related: 1BMF 1COW 1E1Q 1E1R 1E79 1EFR 1H8E 1H8H 1NBM 1OHH 1QO1 1W0J 1W0K 2CK3 2JDI 2JIZ 2JJ1 2JJ2 2V7Q 2W6E 2W6F 2W6G 2W6H 2W6I 2W6J 2WSS
• Descriptor: ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL, SULFATE ION, ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL, ... (10 entities in total)
• Functional Keywords: atp phosphorylase (h+ transporting), atp synthesis, f1fo atp synthase, hydrolase, ion transport, p-loop
• Biological source: BOS TAURUS (BOVINE); More
• Cellular location: Mitochondrion inner membrane (By similarity): P19483; Mitochondrion: P00829 P05631 P05630 P05632; Mitochondrion membrane; Multi-pass membrane protein: P32876
• Total number of polymer chains: 17
• Total formula weight: 421716.11

Authors

Watt, I.N.,Montgomery, M.G.,Runswick, M.J.,Leslie, A.G.W.,Walker, J.E. (deposition date: 2010-08-02, release date: 2010-09-15, Last modification date: 2023-12-20)

Primary citation

Watt, I.N.,Montgomery, M.G.,Runswick, M.J.,Leslie, A.G.W.,Walker, J.E.
Bioenergetic Cost of Making an Adenosine Triphosphate Molecule in Animal Mitochondria.
Proc.Natl.Acad.Sci.USA, 107:16823-, 2010

PubMed Abstract: The catalytic domain of the F-ATPase in mitochondria protrudes into the matrix of the organelle, and is attached to the membrane domain by central and peripheral stalks. Energy for the synthesis of ATP from ADP and phosphate is provided by the transmembrane proton-motive-force across the inner membrane, generated by respiration. The proton-motive force is coupled mechanically to ATP synthesis by the rotation at about 100 times per second of the central stalk and an attached ring of c-subunits in the membrane domain. Each c-subunit carries a glutamate exposed around the midpoint of the membrane on the external surface of the ring. The rotation is generated by protonation and deprotonation successively of each glutamate. Each 360° rotation produces three ATP molecules, and requires the translocation of one proton per glutamate by each c-subunit in the ring. In fungi, eubacteria, and plant chloroplasts, ring sizes of c(10)-c(15) subunits have been observed, implying that these enzymes need 3.3-5 protons to make each ATP, but until now no higher eukaryote has been examined. As shown here in the structure of the bovine F(1)-c-ring complex, the c-ring has eight c-subunits. As the sequences of c-subunits are identical throughout almost all vertebrates and are highly conserved in invertebrates, their F-ATPases probably contain c(8)-rings also. Therefore, in about 50,000 vertebrate species, and probably in many or all of the two million invertebrate species, 2.7 protons are required by the F-ATPase to make each ATP molecule.

PubMed: 20847295
DOI: 10.1073/PNAS.1011099107

Experimental method

X-RAY DIFFRACTION (3.5 Å)