6F34

Crystal structure of a bacterial cationic amino acid transporter (CAT) homologue bound to Arginine.

6F34 の概要

• エントリーDOI: 10.2210/pdb6f34/pdb
• 関連するPDBエントリー: 5OQT
• 分子名称: Amino acid transporter, MgtS, ARGININE, ... (6 entities in total)
• 機能のキーワード: amino acid transporter; slc7, membrane protein
• 由来する生物種: Geobacillus kaustophilus; 詳細
• 細胞内の位置: Cell inner membrane ; Single-pass membrane protein : A5A616
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53899.05

構造登録者

Jungnickel, K.E.J.,Newstead, S. (登録日: 2017-11-27, 公開日: 2018-02-14, 最終更新日: 2024-01-17)

主引用文献

Jungnickel, K.E.J.,Parker, J.L.,Newstead, S.
Structural basis for amino acid transport by the CAT family of SLC7 transporters.
Nat Commun, 9:550-550, 2018

PubMed Abstract: Amino acids play essential roles in cell biology as regulators of metabolic pathways. Arginine in particular is a major signalling molecule inside the cell, being a precursor for both l-ornithine and nitric oxide (NO) synthesis and a key regulator of the mTORC1 pathway. In mammals, cellular arginine availability is determined by members of the solute carrier (SLC) 7 family of cationic amino acid transporters. Whereas CAT-1 functions to supply cationic amino acids for cellular metabolism, CAT-2A and -2B are required for macrophage activation and play important roles in regulating inflammation. Here, we present the crystal structure of a close homologue of the mammalian CAT transporters that reveals how these proteins specifically recognise arginine. Our structural and functional data provide a model for cationic amino acid transport in mammalian cells and reveals mechanistic insights into proton-coupled, sodium-independent amino acid transport in the wider APC superfamily.

PubMed: 29416041
DOI: 10.1038/s41467-018-03066-6

実験手法

X-RAY DIFFRACTION (3.13 Å)