PDBsum entry 5are

Hydrolase

PDB id: 5are

Contents

Protein chains

509 a.a.

480 a.a.

467 a.a.

264 a.a.

131 a.a.

47 a.a.

(+ 2 more) 72 a.a.

168 a.a.

174 a.a.

122 a.a.

67 a.a.

217 a.a.

PDB id:

5are

Name:

Hydrolase

Title:

Bovine mitochondrial atp synthase state 1b

Structure:

Atp synthase subunit alpha, mitochondrial. Chain: a, b, c. Fragment: unp residues 44-553. Atp synthase subunit beta, mitochondrial. Chain: d, e, f. Fragment: unp residues 47-528. Atp synthase subunit gamma, mitochondrial. Chain: g. Fragment: unp residues 26-298.

Source:

Bos taurus. Cow. Organism_taxid: 9913. Organ: mitochondria. Tissue: heart. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: c41. Tissue: heart

Authors:

A.Zhou,A.Rohou,D.G.Schep,J.V.Bason,M.G.Montgomery,J.E.Walker, N.Grigorieff,J.L.Rubinstein

Key ref:

A.Zhou et al. (2015). Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM. Elife, 4, e10180. PubMed id: 26439008 DOI: 10.7554/eLife.10180

Date:

24-Sep-15 Release date: 14-Oct-15

Protein chain

P19483  (ATPA_BOVIN) -  ATP synthase subunit alpha, mitochondrial from Bos taurus

Seq: 553 a.a.

Struc: 509 a.a.*

Protein chains

P19483  (ATPA_BOVIN) -  ATP synthase subunit alpha, mitochondrial from Bos taurus

Seq: 553 a.a.

Struc: 480 a.a.*

Protein chains

P00829  (ATPB_BOVIN) -  ATP synthase subunit beta, mitochondrial from Bos taurus

Seq: 528 a.a.

Struc: 467 a.a.

Protein chain

P05631  (ATPG_BOVIN) -  ATP synthase subunit gamma, mitochondrial from Bos taurus

Seq: 298 a.a.

Struc: 264 a.a.

Protein chain

P05630  (ATPD_BOVIN) -  ATP synthase subunit delta, mitochondrial from Bos taurus

Seq: 168 a.a.

Struc: 131 a.a.

Protein chain

P05632  (ATP5E_BOVIN) -  ATP synthase subunit epsilon, mitochondrial from Bos taurus

Seq: 51 a.a.

Struc: 47 a.a.

Protein chains

P32876  (AT5G1_BOVIN) -  ATP synthase F(0) complex subunit C1, mitochondrial from Bos taurus

Seq: 136 a.a.

Struc: 72 a.a.

Protein chain

P13621  (ATPO_BOVIN) -  ATP synthase subunit O, mitochondrial from Bos taurus

Seq: 213 a.a.

Struc: 168 a.a.*

Protein chain

P13619  (AT5F1_BOVIN) -  ATP synthase F(0) complex subunit B1, mitochondrial from Bos taurus

Seq: 256 a.a.

Struc: 174 a.a.

Protein chain

P13620  (ATP5H_BOVIN) -  ATP synthase subunit d, mitochondrial from Bos taurus

Seq: 161 a.a.

Struc: 122 a.a.

Protein chain

P02721  (ATP5J_BOVIN) -  ATP synthase-coupling factor 6, mitochondrial from Bos taurus

Seq: 108 a.a.

Struc: 67 a.a.

Protein chain

P00847  (ATP6_BOVIN) -  ATP synthase subunit a from Bos taurus

Seq: 226 a.a.

Struc: 217 a.a.

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains D, E, F: E.C.7.1.2.2 - H(+)-transporting two-sector ATPase.
• Reaction: ATP + H2O + 4 H⁺(in) = ADP + phosphate + 5 H⁺(out)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.7554/eLife.10180

Elife 4:e10180 (2015)

PubMed id: 26439008

Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM.

A.Zhou, A.Rohou, D.G.Schep, J.V.Bason, M.G.Montgomery, J.E.Walker, N.Grigorieff, J.L.Rubinstein.

ABSTRACT

Adenosine triphosphate (ATP), the chemical energy currency of biology, is synthesized in eukaryotic cells primarily by the mitochondrial ATP synthase. ATP synthases operate by a rotary catalytic mechanism where proton translocation through the membrane-inserted FO region is coupled to ATP synthesis in the catalytic F1 region via rotation of a central rotor subcomplex. We report here single particle electron cryomicroscopy (cryo-EM) analysis of the bovine mitochondrial ATP synthase. Combining cryo-EM data with bioinformatic analysis allowed us to determine the fold of the a subunit, suggesting a proton translocation path through the FO region that involves both the a and b subunits. 3D classification of images revealed seven distinct states of the enzyme that show different modes of bending and twisting in the intact ATP synthase. Rotational fluctuations of the c8-ring within the FO region support a Brownian ratchet mechanism for proton-translocation-driven rotation in ATP synthases.