4KSS

Crystal Structure of Vibrio cholerae ATPase GspsE Hexamer

4KSS の概要

• エントリーDOI: 10.2210/pdb4kss/pdb
• 関連するPDBエントリー: 4KSR
• 分子名称: Type II secretion system protein E, hemolysin-coregulated protein (1 entity in total)
• 機能のキーワード: t2ss secretion atpase, epse, hexamer, quasi c6 cyclic symmetry, protein transport
• 由来する生物種: Vibrio cholerae O1; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 383566.76

構造登録者

Hol, W.G.,Turley, S.,Lu, C.Y.,Park, Y.J. (登録日: 2013-05-17, 公開日: 2013-09-04, 最終更新日: 2024-02-28)

主引用文献

Lu, C.,Turley, S.,Marionni, S.T.,Park, Y.J.,Lee, K.K.,Patrick, M.,Shah, R.,Sandkvist, M.,Bush, M.F.,Hol, W.G.
Hexamers of the Type II Secretion ATPase GspE from Vibrio cholerae with Increased ATPase Activity.
Structure, 21:1707-1717, 2013

PubMed Abstract: The type II secretion system (T2SS), a multiprotein machinery spanning two membranes in Gram-negative bacteria, is responsible for the secretion of folded proteins from the periplasm across the outer membrane. The critical multidomain T2SS assembly ATPase GspE(EpsE) had not been structurally characterized as a hexamer. Here, four hexamers of Vibrio cholerae GspE(EpsE) are obtained when fused to Hcp1 as an assistant hexamer, as shown with native mass spectrometry. The enzymatic activity of the GspE(EpsE)-Hcp1 fusions is ∼20 times higher than that of a GspE(EpsE) monomer, indicating that increasing the local concentration of GspE(EpsE) by the fusion strategy was successful. Crystal structures of GspE(EpsE)-Hcp1 fusions with different linker lengths reveal regular and elongated hexamers of GspE(EpsE) with major differences in domain orientation within subunits, and in subunit assembly. SAXS studies on GspE(EpsE)-Hcp1 fusions suggest that even further variability in GspE(EpsE) hexamer architecture is likely.

PubMed: 23954505
DOI: 10.1016/j.str.2013.06.027

実験手法

X-RAY DIFFRACTION (7.58 Å)