3GI9

Crystal Structure of ApcT Transporter Bound to 7F11 Monoclonal Fab Fragment

3GI9 の概要

• エントリーDOI: 10.2210/pdb3gi9/pdb
• 関連するPDBエントリー: 3GI8 3GIA
• 分子名称: 7F11 Anti-ApcT Monoclonal Fab Light Chain, 7F11 Anti-ApcT Monoclonal Fab Heavy Chain, Uncharacterized protein MJ0609, ... (4 entities in total)
• 機能のキーワード: membrane protein, transporter, antibody, cell membrane, membrane, transmembrane, transport protein, structural genomics, psi-2, protein structure initiative, new york consortium on membrane protein structure, nycomps
• 由来する生物種: Mus musculus; 詳細
• 細胞内の位置: Cell membrane ; Multi-pass membrane protein : Q58026
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 96599.72

構造登録者

Shaffer, P.L.,Goehring, A.S.,Shankaranarayanan, A.,Gouaux, E.,New York Consortium on Membrane Protein Structure (NYCOMPS) (登録日: 2009-03-05, 公開日: 2009-08-18, 最終更新日: 2024-10-09)

主引用文献

Shaffer, P.L.,Goehring, A.,Shankaranarayanan, A.,Gouaux, E.
Structure and mechanism of a na+-independent amino Acid transporter.
Science, 325:1010-1014, 2009

PubMed Abstract: Amino acid, polyamine, and organocation (APC) transporters are secondary transporters that play essential roles in nutrient uptake, neurotransmitter recycling, ionic homeostasis, and regulation of cell volume. Here, we present the crystal structure of apo-ApcT, a proton-coupled broad-specificity amino acid transporter, at 2.35 angstrom resolution. The structure contains 12 transmembrane helices, with the first 10 consisting of an inverted structural repeat of 5 transmembrane helices like the leucine transporter LeuT. The ApcT structure reveals an inward-facing, apo state and an amine moiety of lysine-158 located in a position equivalent to the sodium ion site Na2 of LeuT. We propose that lysine-158 is central to proton-coupled transport and that the amine group serves the same functional role as the Na2 ion in LeuT, thus demonstrating common principles among proton- and sodium-coupled transporters.

PubMed: 19608859
DOI: 10.1126/science.1176088

実験手法

X-RAY DIFFRACTION (2.48 Å)