2ca5

From Proteopedia

Revision as of 15:58, 5 November 2007

MXIH NEEDLE PROTEIN OF SHIGELLA FLEXNERI (MONOMERIC FORM, RESIDUES 1-78)

Overview

Type III secretion systems are essential virulence determinants for many, Gram-negative bacterial pathogens. The type III secretion system consists, of cytoplasmic, transmembrane, and extracellular domains. The, extracellular domain is a hollow needle protruding above the bacterial, surface and is held within a basal body that traverses both bacterial, membranes. Effector proteins are translocated, via this external needle, directly into host cells, where they subvert normal cell functions to aid, infection. Physical contact with host cells initiates secretion and leads, to formation of a pore, thought to be contiguous with the needle channel, in the host-cell membrane. Here, we report the crystal structure of the, Shigella flexneri needle subunit MxiH and a complete model for the needle, assembly built into our three-dimensional EM reconstruction. The model, combined with mutagenesis data, reveals that signaling of host-cell, contact is relayed through the needle via intersubunit contacts and, suggests a mode of binding for a tip complex.

About this Structure

2CA5 is a Single protein structure of sequence from Shigella flexneri with NA, IPA and GOL as ligands. Structure known Active Site: 1. Full crystallographic information is available from OCA.

Reference

Molecular model of a type III secretion system needle: Implications for host-cell sensing., Deane JE, Roversi P, Cordes FS, Johnson S, Kenjale R, Daniell S, Booy F, Picking WD, Picking WL, Blocker AJ, Lea SM, Proc Natl Acad Sci U S A. 2006 Aug 15;103(33):12529-33. Epub 2006 Aug 3. PMID:16888041

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