5NV9
Substrate-bound outward-open state of a Na+-coupled sialic acid symporter reveals a novel Na+-site
5NV9 の概要
| エントリーDOI | 10.2210/pdb5nv9/pdb |
| 分子名称 | Putative sodium:solute symporter, SODIUM ION, N-acetyl-beta-neuraminic acid, ... (6 entities in total) |
| 機能のキーワード | membrane protein, membrane symporter, sialic acid, outward-open, sodium-coupled |
| 由来する生物種 | Proteus mirabilis (strain HI4320) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 55893.80 |
| 構造登録者 | Wahlgren, W.Y.,North, R.A.,Dunevall, E.,Paz, A.,Goyal, P.,Bisignano, P.,Grabe, M.,Dobson, R.,Abramson, J.,Ramaswamy, S.,Friemann, R. (登録日: 2017-05-03, 公開日: 2018-04-04, 最終更新日: 2024-11-06) |
| 主引用文献 | Wahlgren, W.Y.,Dunevall, E.,North, R.A.,Paz, A.,Scalise, M.,Bisignano, P.,Bengtsson-Palme, J.,Goyal, P.,Claesson, E.,Caing-Carlsson, R.,Andersson, R.,Beis, K.,Nilsson, U.J.,Farewell, A.,Pochini, L.,Indiveri, C.,Grabe, M.,Dobson, R.C.J.,Abramson, J.,Ramaswamy, S.,Friemann, R. Substrate-bound outward-open structure of a Na+-coupled sialic acid symporter reveals a new Na+site. Nat Commun, 9:1753-1753, 2018 Cited by PubMed Abstract: Many pathogenic bacteria utilise sialic acids as an energy source or use them as an external coating to evade immune detection. As such, bacteria that colonise sialylated environments deploy specific transporters to mediate import of scavenged sialic acids. Here, we report a substrate-bound 1.95 Å resolution structure and subsequent characterisation of SiaT, a sialic acid transporter from Proteus mirabilis. SiaT is a secondary active transporter of the sodium solute symporter (SSS) family, which use Na gradients to drive the uptake of extracellular substrates. SiaT adopts the LeuT-fold and is in an outward-open conformation in complex with the sialic acid N-acetylneuraminic acid and two Na ions. One Na binds to the conserved Na2 site, while the second Na binds to a new position, termed Na3, which is conserved in many SSS family members. Functional and molecular dynamics studies validate the substrate-binding site and demonstrate that both Na sites regulate N-acetylneuraminic acid transport. PubMed: 29717135DOI: 10.1038/s41467-018-04045-7 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.95 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






