2ca5: Difference between revisions

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.

2CA5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri] with NA, IPA and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: 1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CA5 OCA].  

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