6GCI

Structure of the bongkrekic acid-inhibited mitochondrial ADP/ATP carrier

6GCI の概要

• エントリーDOI: 10.2210/pdb6gci/pdb
• 分子名称: mitochondrial ADP/ATP carrier, Nanobody, Bongkrekic acid, ... (5 entities in total)
• 機能のキーワード: transporter, inhibitor, mitochondrial, carrier, membrane protein
• 由来する生物種: Thermothelomyces thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 56653.63

構造登録者

Ruprecht, J.J.,King, M.S.,Pardon, E.,Aleksandrova, A.A.,Zogg, T.,Crichton, P.G.,Steyaert, J.,Kunji, E.R.S. (登録日: 2018-04-17, 公開日: 2019-01-09, 最終更新日: 2024-11-13)

主引用文献

Ruprecht, J.J.,King, M.S.,Zogg, T.,Aleksandrova, A.A.,Pardon, E.,Crichton, P.G.,Steyaert, J.,Kunji, E.R.S.
The Molecular Mechanism of Transport by the Mitochondrial ADP/ATP Carrier.
Cell, 176:435-447.e15, 2019

PubMed 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.

PubMed: 30611538
DOI: 10.1016/j.cell.2018.11.025

実験手法

X-RAY DIFFRACTION (3.3 Å)