2bh1

From Proteopedia

Revision as of 14:32, 30 October 2007

X-RAY STRUCTURE OF THE GENERAL SECRETION PATHWAY COMPLEX OF THE N-TERMINAL DOMAIN OF EPSE AND THE CYTOSOLIC DOMAIN OF EPSL OF VIBRIO CHOLERAE

Overview

Gram-negative bacteria use type II secretion systems for the transport of, virulence factors and hydrolytic enzymes through the outer membrane. These, sophisticated multi-protein complexes reach from the pore in the outer, membrane via the pseudopilins in the periplasm and a multi-protein, inner-membrane sub-complex, to an ATPase in the cytoplasm. The human, pathogen Vibrio cholerae uses such a secretion machinery, called the, Eps-system, for the export of its major virulence factor cholera toxin, into the intestinal tract of the human host. Here, we describe the 2.4 A, structure of the hetero-tetrameric complex of the N-terminal domain of the, ATPase EpsE and the cytoplasmic domain of the inner membrane protein EpsL, which constitute the major cytoplasmic components of the Eps-system. A, ... [(full description)]

About this Structure

2BH1 is a [Protein complex] structure of sequences from [Vibrio cholerae] with CA as [ligand]. Structure known Active Site: CAL. Full crystallographic information is available from [OCA].

Reference

The X-ray structure of the type II secretion system complex formed by the N-terminal domain of EpsE and the cytoplasmic domain of EpsL of Vibrio cholerae., Abendroth J, Murphy P, Sandkvist M, Bagdasarian M, Hol WG, J Mol Biol. 2005 May 13;348(4):845-55. PMID:15843017

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