2C3E

The bovine mitochondrial ADP-ATP carrier

2C3E の概要

• エントリーDOI: 10.2210/pdb2c3e/pdb
• 関連するPDBエントリー: 1OKC
• 分子名称: ADP/ATP TRANSLOCASE 1, Carboxyatractyloside, CARDIOLIPIN (3 entities in total)
• 機能のキーワード: mitochondrial carrier, nucleotide transport, membrane 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: 38042.19

構造登録者

Nury, H.,Dahout-Gonzalez, C.,Trezeguet, V.,Lauquin, G.,Brandolin, G.,Pebay-Peyroula, E. (登録日: 2005-10-06, 公開日: 2005-10-20, 最終更新日: 2023-12-13)

主引用文献

Nury, H.,Dahout-Gonzalez, C.,Trezeguet, V.,Lauquin, G.,Brandolin, G.,Pebay-Peyroula, E.
Structural Basis for Lipid-Mediated Interactions between Mitochondrial Adp/ATP Carrier Monomers.
FEBS Lett., 579:6031-, 2005

PubMed Abstract: The oligomerization state of the ADP/ATP carrier is an important issue in understanding the mechanism underlying nucleotide exchange across the inner mitochondrial membrane. The first high resolution structure obtained in the presence of carboxyatractyloside revealed a large cavity formed within a monomer in which the inhibitor is strongly bound. Whereas the protein-protein interactions implicated in the first crystal form are not biologically relevant, the new crystal form described herein, highlights favorable protein-protein interactions. The interactions are mediated by endogenous cardiolipins, which are tightly bound to the protein, two cardiolipins being sandwiched between the monomers on the matrix side. The putative dimerization interface evidenced here is consistent with other structural, biochemical or functional data published so far.

PubMed: 16226253
DOI: 10.1016/J.FEBSLET.2005.09.061

実験手法

X-RAY DIFFRACTION (2.8 Å)