PDBsum entry 2xnd

Hydrolase

PDB id: 2xnd

Contents

Protein chains

492 a.a. *

467 a.a. *

263 a.a. *

131 a.a. *

47 a.a. *

(+ 2 more) 72 a.a. *

Ligands

ANP ×5

GOL

SO4

Metals

_MG ×5

* Residue conservation analysis

PDB id:

2xnd

Name:

Hydrolase

Title:

Crystal structure of bovine f1-c8 sub-complex of atp synthase

Structure:

Atp synthase subunit alpha, mitochondrial. Chain: a, b, c. Fragment: residues 62-553. Atp synthase subunit beta, mitochondrial. Chain: d, e, f. Fragment: residues 59-525. Atp synthase subunit gamma, mitochondrial. Chain: g. Fragment: residues 26-297.

Source:

Bos taurus. Bovine. Organism_taxid: 9913. Organ: heart. Tissue: muscle. Tissue: muscle

Resolution:

3.50Å R-factor: 0.263 R-free: 0.304

Authors:

I.N.Watt,M.G.Montgomery,M.J.Runswick,A.G.W.Leslie,J.E.Walker

Key ref:

I.N.Watt et al. (2010). Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria. Proc Natl Acad Sci U S A, 107, 16823-16827. PubMed id: 20847295

Date:

02-Aug-10 Release date: 15-Sep-10

Protein chains

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

Seq: 553 a.a.

Struc: 492 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: 263 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.

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class 2: Chains A, B, C, G, H, I, J, K, L, M, N, O, P, Q: E.C.3.6.3.14 - Transferred entry: 7.1.2.2.
• Reaction: ATP + H₂O + H⁺(In) = ADP + phosphate + H⁺(Out)

ATP + H(2)O + H(+)(In) = ADP (Bound ligand (Het Group name = ANP) matches with 81.25% similarity) + phosphate + H(+)(Out)

• Enzyme class 3: 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)

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

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

reference

Proc Natl Acad Sci U S A 107:16823-16827 (2010)

PubMed id: 20847295

Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria.

I.N.Watt, M.G.Montgomery, M.J.Runswick, A.G.Leslie, J.E.Walker.

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.