1p9r: Difference between revisions
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[[Image:1p9r.jpg|left|200px]] | [[Image:1p9r.jpg|left|200px]] | ||
'''Crystal Structure of Vibrio cholerae putative NTPase EpsE''' | {{Structure | ||
|PDB= 1p9r |SIZE=350|CAPTION= <scene name='initialview01'>1p9r</scene>, resolution 2.50Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | |||
|ACTIVITY= | |||
|GENE= EPSE OR VC2732 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=666 Vibrio cholerae]) | |||
}} | |||
'''Crystal Structure of Vibrio cholerae putative NTPase EpsE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1P9R is a [ | 1P9R is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P9R OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of the extracellular protein secretion NTPase EpsE of Vibrio cholerae., Robien MA, Krumm BE, Sandkvist M, Hol WG, J Mol Biol. 2003 Oct 24;333(3):657-74. PMID:[http:// | Crystal structure of the extracellular protein secretion NTPase EpsE of Vibrio cholerae., Robien MA, Krumm BE, Sandkvist M, Hol WG, J Mol Biol. 2003 Oct 24;333(3):657-74. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14556751 14556751] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Vibrio cholerae]] | [[Category: Vibrio cholerae]] | ||
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[[Category: putative atpase/ atp binding protein]] | [[Category: putative atpase/ atp binding protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:21:48 2008'' |
Revision as of 14:21, 20 March 2008
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, resolution 2.50Å | |||||||
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Ligands: | and | ||||||
Gene: | EPSE OR VC2732 (Vibrio cholerae) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal Structure of Vibrio cholerae putative NTPase EpsE
OverviewOverview
Type II secretion systems consist of an assembly of 12-15 Gsp proteins responsible for transporting a variety of virulence factors across the outer membrane in several pathogenic bacteria. In Vibrio cholerae, the major virulence factor cholera toxin is secreted by the Eps Type II secretion apparatus consisting of 14 Eps proteins. One of these, EpsE, is a cytoplasmic putative NTPase essential for the functioning of the Eps system and member of the GspE subfamily of Type II secretion ATPases. The crystal structure of a truncated form of EpsE in nucleotide-liganded and unliganded state has been determined, and reveals a two-domain architecture with the four characteristic sequence "boxes" of the GspE subfamily clustering around the nucleotide-binding site of the C-domain. This domain contains two C-terminal subdomains not reported before in this superfamily of NTPases. One of these subdomains contains a four-cysteine motif that appears to be involved in metal binding as revealed by anomalous difference density. The EpsE subunits form a right-handed helical arrangement in the crystal with extensive and conserved contacts between the C and N domains of neighboring subunits. Combining the most conserved interface with the quaternary structure of the C domain in a distant homolog, a hexameric model for EpsE is proposed which may reflect the assembly of this critical protein in the Type II secretion system. The nucleotide ligand contacts both domains in this model. The N2-domain-containing surface of the hexamer appears to be highly conserved in the GspE family and most likely faces the inner membrane interacting with other members of the Eps system.
About this StructureAbout this Structure
1P9R is a Single protein structure of sequence from Vibrio cholerae. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the extracellular protein secretion NTPase EpsE of Vibrio cholerae., Robien MA, Krumm BE, Sandkvist M, Hol WG, J Mol Biol. 2003 Oct 24;333(3):657-74. PMID:14556751
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