1OKC

structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside

1OKC の概要

• エントリーDOI: 10.2210/pdb1okc/pdb
• 分子名称: ADP, ATP CARRIER PROTEIN HEART ISOFORM T1, Carboxyatractyloside, CARDIOLIPIN, ... (6 entities in total)
• 機能のキーワード: mitochondrial transporter, nucleotide translocation, membrane protein, carrier protein, transport protein
• 由来する生物種: BOS TAURUS (CATTLE)
• 細胞内の位置: Mitochondrion inner membrane; Multi-pass membrane protein: P02722
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41803.73

構造登録者

Pebay-Peyroula, E.,Dahout-Gonzalez, C.,Kahn, R.,Trezeguet, V.,Lauquin, G.J.-M.,Brandolin, G. (登録日: 2003-07-21, 公開日: 2003-11-07, 最終更新日: 2024-05-08)

主引用文献

Pebay-Peyroula, E.,Dahout-Gonzalez, C.,Kahn, R.,Trezeguet, V.,Lauquin, G.J.-M.,Brandolin, G.
Structure of Mitochondrial Adp/ATP Carrier in Complex with Carboxyatractyloside
Nature, 426:39-, 2003

PubMed Abstract: ATP, the principal energy currency of the cell, fuels most biosynthetic reactions in the cytoplasm by its hydrolysis into ADP and inorganic phosphate. Because resynthesis of ATP occurs in the mitochondrial matrix, ATP is exported into the cytoplasm while ADP is imported into the matrix. The exchange is accomplished by a single protein, the ADP/ATP carrier. Here we have solved the bovine carrier structure at a resolution of 2.2 A by X-ray crystallography in complex with an inhibitor, carboxyatractyloside. Six alpha-helices form a compact transmembrane domain, which, at the surface towards the space between inner and outer mitochondrial membranes, reveals a deep depression. At its bottom, a hexapeptide carrying the signature of nucleotide carriers (RRRMMM) is located. Our structure, together with earlier biochemical results, suggests that transport substrates bind to the bottom of the cavity and that translocation results from a transient transition from a 'pit' to a 'channel' conformation.

PubMed: 14603310
DOI: 10.1038/NATURE02056

実験手法

X-RAY DIFFRACTION (2.2 Å)