3HE1

Secreted protein Hcp3 from Pseudomonas aeruginosa.

Summary for 3HE1

• Entry DOI: 10.2210/pdb3he1/pdb
• Descriptor: Major exported Hcp3 protein, GLYCEROL (3 entities in total)
• Functional Keywords: structural genomics, apc22128, hcp3, hcpc, secretion, virulence, psi-2, protein structure initiative, midwest center for structural genomics, mcsg, secreted, unknown function
• Biological source: Pseudomonas aeruginosa
• Cellular location: Secreted : Q9HI36
• Total number of polymer chains: 6
• Total formula weight: 132211.22

Authors

Osipiuk, J.,Xu, X.,Cui, H.,Savchenko, A.,Edwards, A.M.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2009-05-07, release date: 2009-06-16, Last modification date: 2017-11-01)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.098 Å)