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2YN3

Structural insight into the giant calcium-binding adhesin SiiE: implications for the adhesion of Salmonella enterica to polarized epithelial cells

2YN3 の概要
エントリーDOI10.2210/pdb2yn3/pdb
関連するPDBエントリー2YN5
分子名称PUTATIVE INNER MEMBRANE PROTEIN, IODIDE ION, CALCIUM ION, ... (5 entities in total)
機能のキーワードmembrane protein, big-domains adhesin
由来する生物種SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM
タンパク質・核酸の鎖数4
化学式量合計122556.58
構造登録者
主引用文献Griessl, M.H.,Schmid, B.,Kassler, K.,Braunsmann, C.,Ritter, R.,Barlag, B.,Stierhof, Y.,Sturm, K.U.,Danzer, C.,Wagner, C.,Schaffer, T.E.,Sticht, H.,Hensel, M.,Muller, Y.A.
Structural Insight Into the Giant Ca(2+)-Binding Adhesin Siie: Implications for the Adhesion of Salmonella Enterica to Polarized Epithelial Cells.
Structure, 21:741-, 2013
Cited by
PubMed Abstract: SiiE from Salmonella enterica is a giant 5,559-residue-long nonfimbrial adhesin that is secreted by a type 1 secretion system (T1SS) and initiates bacterial adhesion to polarized host cells. Structural insight has been gained into the 53 bacterial Ig-like (BIg) domains of SiiE, which account for 94% of the entire SiiE sequence. The crystal structure of a fragment comprising BIg domains 50 to 52 of SiiE reveals the BIg domain architecture and highlights two types of SiiE-specific Ca²⁺-binding sites. Sequence homology considerations suggest that full-length SiiE interacts with more than 100 Ca²⁺ ions. Molecular dynamics simulations and single-molecule imaging indicate that Ca²⁺ binding confers SiiE with a rigid 200 nm rod-like habitus that is required to reach out beyond the Salmonella lipopolysaccharide layer and to promote adhesion to host cells. The crystal structure suggests plausible routes for the establishment of the initial contact between Salmonella and host cells.
PubMed: 23562396
DOI: 10.1016/J.STR.2013.02.020
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.12 Å)
構造検証レポート
Validation report summary of 2yn3
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-03-04に公開中

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