3QF4

Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation

3QF4 の概要

• エントリーDOI: 10.2210/pdb3qf4/pdb
• 関連するPDBエントリー: 3QF5
• 分子名称: ABC transporter, ATP-binding protein, Uncharacterized ABC transporter ATP-binding protein TM_0288, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (5 entities in total)
• 機能のキーワード: multidrug transporter, transport protein
• 由来する生物種: Thermotoga maritima; 詳細
• 細胞内の位置: Cell membrane ; Multi-pass membrane protein : Q9WYC4
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 133381.17

構造登録者

Hohl, M.,Briand, C.,Gruetter, M.G.,Seeger, M.A. (登録日: 2011-01-21, 公開日: 2012-03-28, 最終更新日: 2024-03-20)

主引用文献

Hohl, M.,Briand, C.,Grutter, M.G.,Seeger, M.A.
Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation
Nat.Struct.Mol.Biol., 19:395-402, 2012

PubMed Abstract: ATP-binding cassette (ABC) transporters shuttle a wide variety of molecules across cell membranes by alternating between inward- and outward-facing conformations, harnessing the energy of ATP binding and hydrolysis at their nucleotide binding domains (NBDs). Here we present the 2.9-Å crystal structure of the heterodimeric ABC transporter TM287-TM288 (TM287/288) from Thermotoga maritima in its inward-facing state. In contrast to previous studies, we found that the NBDs only partially separate, remaining in contact through an interface involving conserved motifs that connect the two ATP hydrolysis sites. We observed AMP-PNP binding to the degenerate catalytic site, which deviates from the consensus sequence in the same positions as the eukaryotic homologs CFTR and TAP1-TAP2 (TAP1/2). The TM287/288 structure provides unprecedented insights into the mechanism of heterodimeric ABC exporters and will enable future studies on this large transporter superfamily.

PubMed: 22447242
DOI: 10.1038/nsmb.2267

実験手法

X-RAY DIFFRACTION (2.9 Å)