3HE1

Secreted protein Hcp3 from Pseudomonas aeruginosa.

3HE1 の概要

• エントリーDOI: 10.2210/pdb3he1/pdb
• 分子名称: Major exported Hcp3 protein, GLYCEROL (3 entities in total)
• 機能のキーワード: structural genomics, apc22128, hcp3, hcpc, secretion, virulence, psi-2, protein structure initiative, midwest center for structural genomics, mcsg, secreted, unknown function
• 由来する生物種: Pseudomonas aeruginosa
• 細胞内の位置: Secreted : Q9HI36
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 132211.22

構造登録者

Osipiuk, J.,Xu, X.,Cui, H.,Savchenko, A.,Edwards, A.M.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (登録日: 2009-05-07, 公開日: 2009-06-16, 最終更新日: 2017-11-01)

主引用文献

Osipiuk, J.,Xu, X.,Cui, H.,Savchenko, A.,Edwards, A.,Joachimiak, A.
Crystal structure of secretory protein Hcp3 from Pseudomonas aeruginosa.
J.Struct.Funct.Genom., 12:21-26, 2011

PubMed Abstract: The Type VI secretion pathway transports proteins across the cell envelope of Gram-negative bacteria. Pseudomonas aeruginosa, an opportunistic Gram-negative bacterial pathogen infecting humans, uses the type VI secretion pathway to export specific effector proteins crucial for its pathogenesis. The HSI-I virulence locus encodes for several proteins that has been proposed to participate in protein transport including the Hcp1 protein, which forms hexameric rings that assemble into nanotubes in vitro. Two Hcp1 paralogues have been identified in the P. aeruginosa genome, Hsp2 and Hcp3. Here, we present the structure of the Hcp3 protein from P. aeruginosa. The overall structure of the monomer resembles Hcp1 despite the lack of amino-acid sequence similarity between the two proteins. The monomers assemble into hexamers similar to Hcp1. However, instead of forming nanotubes in head-to-tail mode like Hcp1, Hcp3 stacks its rings in head-to-head mode forming double-ring structures.

PubMed: 21476004
DOI: 10.1007/s10969-011-9107-1

実験手法

X-RAY DIFFRACTION (2.098 Å)