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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DOI10.2210/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: 29717135
DOI: 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
Validation report summary of 5nv9
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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