2bh1
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(New page: 200px<br /> <applet load="2bh1" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bh1, resolution 2.40Å" /> '''X-RAY STRUCTURE OF ...)
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Revision as of 17:05, 29 October 2007
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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]. 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
Page seeded by OCA on Mon Oct 29 19:10:13 2007
Categories: Protein complex | Vibrio cholerae | Abendroth, J. | Bagdasarian, M. | Hol, W.G.J. | Murphy, P.M. | Mushtaq, A. | Sandkvist, M. | CA | Atp-binding | Eps | Gsp | Transmembrane | Transport | Type ii secretion