PDBsum entry 4tt3

Hydrolase

PDB id: 4tt3

Contents

Protein chains

487 a.a.

469 a.a.

183 a.a.

40 a.a.

28 a.a.

19 a.a.

Ligands

ATP ×3

GOL ×2

ADP ×2

Metals

_MG ×5

Waters ×28

PDB id:

4tt3

Name:

Hydrolase

Title:

The pathway of binding of the intrinsically disordered mitochondrial inhibitor protein to f1-atpase

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, i, j.

Source:

Bos taurus. Bovine. Organism_taxid: 9913. Organ: heart. Tissue: muscle. Gene: atpif1, atpi. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

3.21Å R-factor: 0.244 R-free: 0.283

Authors:

J.V.Bason,M.G.Montgomery,A.G.W.Leslie,J.E.Walker

Key ref:

J.V.Bason et al. (2014). Pathway of binding of the intrinsically disordered mitochondrial inhibitor protein to F1-ATPase. Proc Natl Acad Sci U S A, 111, 11305-11310. PubMed id: 25049402 DOI: 10.1073/pnas.1411560111

Date:

19-Jun-14 Release date: 06-Aug-14

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: 183 a.a.

Protein chain

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

Seq: 109 a.a.

Struc: 40 a.a.*

Protein chain

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

Seq: 109 a.a.

Struc: 28 a.a.*

Protein chain

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

Seq: 109 a.a.

Struc: 19 a.a.*

* PDB and UniProt seqs differ at 4 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 (Bound ligand (Het Group name = ATP) corresponds exactly) + H2O + 4 × H(+)(in) = ADP + phosphate + 5 × H(+)(out)

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

reference

DOI no: 10.1073/pnas.1411560111

Proc Natl Acad Sci U S A 111:11305-11310 (2014)

PubMed id: 25049402

Pathway of binding of the intrinsically disordered mitochondrial inhibitor protein to F1-ATPase.

J.V.Bason, M.G.Montgomery, A.G.Leslie, J.E.Walker.

ABSTRACT

The hydrolysis of ATP by the ATP synthase in mitochondria is inhibited by a protein called IF1. Bovine IF1 has 84 amino acids, and its N-terminal inhibitory region is intrinsically disordered. In a known structure of bovine F1-ATPase inhibited with residues 1-60 of IF1, the inhibitory region from residues 1-50 is mainly α-helical and buried deeply at the αDPβDP-catalytic interface, where it forms extensive interactions with five of the nine subunits of F1-ATPase but mainly with the βDP-subunit. As described here, on the basis of two structures of inhibited complexes formed in the presence of large molar excesses of residues 1-60 of IF1 and of a version of IF1 with the mutation K39A, it appears that the intrinsically disordered inhibitory region interacts first with the αEβE-catalytic interface, the most open of the three catalytic interfaces, where the available interactions with the enzyme allow it to form an α-helix from residues 31-49. Then, in response to the hydrolysis of an ATP molecule and the associated partial closure of the interface to the αTPβTP state, the extent of the folded α-helical region of IF1 increases to residues 23-50 as more interactions with the enzyme become possible. Finally, in response to the hydrolysis of a second ATP molecule and a concomitant 120° rotation of the γ-subunit, the interface closes further to the αDPβDP-state, allowing more interactions to form between the enzyme and IF1. The structure of IF1 now extends to its maximally folded state found in the previously observed inhibited complex.