6CSE

Crystal structure of sodium/alanine symporter AgcS with L-alanine bound

6CSE の概要

• エントリーDOI: 10.2210/pdb6cse/pdb
• 分子名称: Monoclonal antibody FAB heavy chain, Monoclonal antibody FAB light chain, Sodium/alanine symporter AgcS, ... (5 entities in total)
• 機能のキーワード: membrane protein
• 由来する生物種: Methanococcus maripaludis (strain S2 / LL); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 185443.29

構造登録者

Ma, J.,Reyes, F.E.,Gonen, T. (登録日: 2018-03-20, 公開日: 2019-01-30, 最終更新日: 2024-11-13)

主引用文献

Ma, J.,Lei, H.T.,Reyes, F.E.,Sanchez-Martinez, S.,Sarhan, M.F.,Hattne, J.,Gonen, T.
Structural basis for substrate binding and specificity of a sodium-alanine symporter AgcS.
Proc. Natl. Acad. Sci. U.S.A., 116:2086-2090, 2019

PubMed Abstract: The amino acid, polyamine, and organocation (APC) superfamily is the second largest superfamily of membrane proteins forming secondary transporters that move a range of organic molecules across the cell membrane. Each transporter in the APC superfamily is specific for a unique subset of substrates, even if they possess a similar structural fold. The mechanism of substrate selectivity remains, by and large, elusive. Here, we report two crystal structures of an APC member from , the alanine or glycine:cation symporter (AgcS), with l- or d-alanine bound. Structural analysis combined with site-directed mutagenesis and functional studies inform on substrate binding, specificity, and modulation of the AgcS family and reveal key structural features that allow this transporter to accommodate glycine and alanine while excluding all other amino acids. Mutation of key residues in the substrate binding site expand the selectivity to include valine and leucine. These studies provide initial insights into substrate selectivity in AgcS symporters.

PubMed: 30659158
DOI: 10.1073/pnas.1806206116

実験手法

X-RAY DIFFRACTION (3.24 Å)