2YNK

Wzi, an Outer Membrane Protein Involved in Group 1 Capsule Assembly in Escherichia coli, is a Carbohydrate Binding Beta-Barrel

2YNK の概要

• エントリーDOI: 10.2210/pdb2ynk/pdb
• 分子名称: WZI, N-OCTANE, DODECANE, ... (5 entities in total)
• 機能のキーワード: membrane protein, capsule export
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 53398.42

構造登録者

Bushell, S.R.,Mainprize, I.L.,Wear, M.A.,Lou, H.,Kong, L.,Davis, B.,Bayley, H.,Whitfield, C.,Naismith, J.H. (登録日: 2012-10-16, 公開日: 2013-05-15, 最終更新日: 2024-11-20)

主引用文献

Bushell, S.R.,Mainprize, I.L.,Wear, M.A.,Lou, H.,Whitfield, C.,Naismith, J.H.
Wzi is an Outer Membrane Lectin that Underpins Group 1 Capsule Assembly in Escherichia Coli.
Structure, 21:844-, 2013

PubMed Abstract: Many pathogenic bacteria encase themselves in a polysaccharide capsule that provides a barrier to the physical and immunological challenges of the host. The mechanism by which the capsule assembles around the bacterial cell is unknown. Wzi, an integral outer-membrane protein from Escherichia coli, has been implicated in the formation of group 1 capsules. The 2.6 Å resolution structure of Wzi reveals an 18-stranded β-barrel fold with a novel arrangement of long extracellular loops that blocks the extracellular entrance and a helical bundle that plugs the periplasmic end. Mutagenesis shows that specific extracellular loops are required for in vivo capsule assembly. The data show that Wzi binds the K30 carbohydrate polymer and, crucially, that mutants functionally deficient in vivo show no binding to K30 polymer in vitro. We conclude that Wzi is a novel outer-membrane lectin that assists in the formation of the bacterial capsule via direct interaction with capsular polysaccharides.

PubMed: 23623732
DOI: 10.1016/J.STR.2013.03.010

実験手法

X-RAY DIFFRACTION (2.64 Å)