PDBsum entry 6gci

Membrane protein

PDB id: 6gci

Contents

Protein chains

292 a.a.

124 a.a.

Ligands

BKC

CDL ×5

P6G

PDB id:

6gci

Name:

Membrane protein

Title:

Structure of the bongkrekic acid-inhibited mitochondrial adp/atp carrier

Structure:

Mitochondrial adp/atp carrier. Chain: a. Engineered: yes. Mutation: yes. Other_details: sequence has q302k mutation. Nanobody. Chain: b. Engineered: yes. Other_details: nanobody selected against the bka-inhibited adp/atp

Source:

Thermothelomyces thermophila (strain atcc 42464 / bcrc 31852 / dsm 1799). Sporotrichum thermophile. Organism_taxid: 573729. Strain: atcc 42464 / bcrc 31852 / dsm 1799. Atcc: 42464. Gene: mycth_2316753. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.

Resolution:

3.30Å R-factor: 0.253 R-free: 0.283

Authors:

J.J.Ruprecht,M.S.King,E.Pardon,A.A.Aleksandrova,T.Zogg,P.G.Crichton, J.Steyaert,E.R.S.Kunji

Key ref:

J.J.Ruprecht et al. (2019). The Molecular Mechanism of Transport by the Mitochondrial ADP/ATP Carrier. Cell, 176, 435. PubMed id: 30611538 DOI: 10.1016/j.cell.2018.11.025

Date:

17-Apr-18 Release date: 09-Jan-19

Protein chain

G2QNH0  (G2QNH0_MYCTT) -  ADP/ATP translocase from Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799)

Seq: 315 a.a.

Struc: 292 a.a.*

Protein chain

No UniProt id for this chain

Struc: 124 a.a.

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

DOI no: 10.1016/j.cell.2018.11.025

Cell 176:435 (2019)

PubMed id: 30611538

The Molecular Mechanism of Transport by the Mitochondrial ADP/ATP Carrier.

J.J.Ruprecht, M.S.King, T.Zögg, A.A.Aleksandrova, E.Pardon, P.G.Crichton, J.Steyaert, E.R.S.Kunji.

ABSTRACT

Mitochondrial ADP/ATP carriers transport ADP into the mitochondrial matrix for ATP synthesis, and ATP out to fuel the cell, by cycling between cytoplasmic-open and matrix-open states. The structure of the cytoplasmic-open state is known, but it has proved difficult to understand the transport mechanism in the absence of a structure in the matrix-open state. Here, we describe the structure of the matrix-open state locked by bongkrekic acid bound in the ADP/ATP-binding site at the bottom of the central cavity. The cytoplasmic side of the carrier is closed by conserved hydrophobic residues, and a salt bridge network, braced by tyrosines. Glycine and small amino acid residues allow close-packing of helices on the matrix side. Uniquely, the carrier switches between states by rotation of its three domains about a fulcrum provided by the substrate-binding site. Because these features are highly conserved, this mechanism is likely to apply to the whole mitochondrial carrier family. VIDEO ABSTRACT.