PDBsum entry 3zdq

Hydrolase

PDB id: 3zdq

Contents

Protein chain

570 a.a.

Ligands

GLY

LMT ×3

CDL ×2

Waters ×30

PDB id:

3zdq

Name:

Hydrolase

Title:

Structure of the human mitochondrial abc transporter, abcb10 (nucleotide-free form)

Structure:

Atp-binding cassette sub-family b member 10, mitochondrial. Chain: a. Fragment: abc transporter, residues 152-738. Synonym: atp-binding cassette transporter 10, abc transporter 10 protein, mitochondrial atp-binding cassette 2, m-abc2, atp-binding cassette sub-family b member 10. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf9.

Resolution:

2.85Å R-factor: 0.204 R-free: 0.244

Authors:

A.C.W.Pike,C.A.Shintre,T.Krojer,F.Von Delft,M.Vollmar,S.Mukhopadhyay, N.Burgess-Brown,C.H.Arrowsmith,C.Bountra,A.M.Edwards,E.P.Carpenter

Key ref:

C.A.Shintre et al. (2013). Structures of ABCB10, a human ATP-binding cassette transporter in apo- and nucleotide-bound states. Proc Natl Acad Sci U S A, 110, 9710-9715. PubMed id: 23716676 DOI: 10.1073/pnas.1217042110

Date:

30-Nov-12 Release date: 23-Jan-13

Protein chain

Q9NRK6  (ABCBA_HUMAN) -  ATP-binding cassette sub-family B member 10, mitochondrial from Homo sapiens

Seq: 738 a.a.

Struc: 570 a.a.

Enzyme reactions

• Enzyme class: E.C.7.6.2.- - ?????

DOI no: 10.1073/pnas.1217042110

Proc Natl Acad Sci U S A 110:9710-9715 (2013)

PubMed id: 23716676

Structures of ABCB10, a human ATP-binding cassette transporter in apo- and nucleotide-bound states.

C.A.Shintre, A.C.Pike, Q.Li, J.I.Kim, A.J.Barr, S.Goubin, L.Shrestha, J.Yang, G.Berridge, J.Ross, P.J.Stansfeld, M.S.Sansom, A.M.Edwards, C.Bountra, B.D.Marsden, F.von Delft, A.N.Bullock, O.Gileadi, N.A.Burgess-Brown, E.P.Carpenter.

ABSTRACT

ABCB10 is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria. In mammals ABCB10 is essential for erythropoiesis, and for protection of mitochondria against oxidative stress. ABCB10 is therefore a potential therapeutic target for diseases in which increased mitochondrial reactive oxygen species production and oxidative stress play a major role. The crystal structure of apo-ABCB10 shows a classic exporter fold ABC transporter structure, in an open-inwards conformation, ready to bind the substrate or nucleotide from the inner mitochondrial matrix or membrane. Unexpectedly, however, ABCB10 adopts an open-inwards conformation when complexed with nonhydrolysable ATP analogs, in contrast to other transporter structures which adopt an open-outwards conformation in complex with ATP. The three complexes of ABCB10/ATP analogs reported here showed varying degrees of opening of the transport substrate binding site, indicating that in this conformation there is some flexibility between the two halves of the protein. These structures suggest that the observed plasticity, together with a portal between two helices in the transmembrane region of ABCB10, assist transport substrate entry into the substrate binding cavity. These structures indicate that ABC transporters may exist in an open-inwards conformation when nucleotide is bound. We discuss ways in which this observation can be aligned with the current views on mechanisms of ABC transporters.