PDBsum entry 1ohh

Synthase

PDB id: 1ohh

Contents

Protein chains

487 a.a. *

469 a.a. *

94 a.a. *

37 a.a. *

Ligands

ANP ×5

Metals

_MG ×5

* Residue conservation analysis

PDB id:

1ohh

Name:

Synthase

Title:

Bovine mitochondrial f1-atpase complexed with the inhibitor protein if1

Structure:

Atp synthase subunit alpha, mitochondrial. Chain: a, b, c. Atp synthase subunit beta, mitochondrial. Chain: d, e, f. Atp synthase subunit gamma, mitochondrial. Chain: g. Synonym: f-atpase gamma subunit. Atpase inhibitor, mitochondrial. Chain: h.

Source:

Bos taurus. Bovine. Organism_taxid: 9913. Organ: heart. Tissue: muscle. Gene: atpif1, atpi. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: c41

Biol. unit:

Octamer (from PDB file)

Resolution:

2.80Å R-factor: 0.232 R-free: 0.280

Ensemble:

2 models

Authors:

E.Cabezon,M.G.Montgomery,A.G.W.Leslie,J.E.Walker

Key ref:

E.Cabezón et al. (2003). The structure of bovine F1-ATPase in complex with its regulatory protein IF1. Nat Struct Biol, 10, 744-750. PubMed id: 12923572 DOI: 10.1038/nsb966

Date:

27-May-03 Release date: 09-Jun-03

Protein chains

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

Seq: 553 a.a.

Struc: 487 a.a.*

Protein chains

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

Seq: 528 a.a.

Struc: 469 a.a.

Protein chain

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

Seq: 298 a.a.

Struc: 94 a.a.*

Protein chain

P01096  (ATIF1_BOVIN) -  ATPase inhibitor, mitochondrial from Bos taurus

Seq: 109 a.a.

Struc: 37 a.a.

* PDB and UniProt seqs differ at 38 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)

ATP + H2O + 4 × H(+)(in) = ADP (Bound ligand (Het Group name = ANP) matches with 81.25% similarity) + phosphate + 5 × H(+)(out)

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

reference

DOI no: 10.1038/nsb966

Nat Struct Biol 10:744-750 (2003)

PubMed id: 12923572

The structure of bovine F1-ATPase in complex with its regulatory protein IF1.

E.Cabezón, M.G.Montgomery, A.G.Leslie, J.E.Walker.

ABSTRACT

In mitochondria, the hydrolytic activity of ATP synthase is prevented by an inhibitor protein, IF1. The active bovine protein (84 amino acids) is an alpha-helical dimer with monomers associated via an antiparallel alpha-helical coiled coil composed of residues 49-81. The N-terminal inhibitory sequences in the active dimer bind to two F1-ATPases in the presence of ATP. In the crystal structure of the F1-IF1 complex at 2.8 A resolution, residues 1-37 of IF1 bind in the alpha(DP)-beta(DP) interface of F1-ATPase, and also contact the central gamma subunit. The inhibitor opens the catalytic interface between the alpha(DP) and beta(DP) subunits relative to previous structures. The presence of ATP in the catalytic site of the beta(DP) subunit implies that the inhibited state represents a pre-hydrolysis step on the catalytic pathway of the enzyme.

Selected figure(s)

Figure 3.
Figure 3. Stereo view of the contacts between F[1]-ATPase and IF[1]. Side chains from residues involved in contacts between F[1]-ATPase and IF[1] have been drawn. For details of the color scheme see the legend to Figure 1.

Figure 6.
Figure 6. The inhibition of the ATP hydrolytic activity of ATP synthase by IF[1]. The scheme is based on the binding change mechanism of ATP hydrolysis26. See text for further details.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2003, 10, 744-750) copyright 2003.

Figures were selected by an automated process.