1i78: Difference between revisions

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[[Image:1i78.jpg|left|200px]]
{{Seed}}
[[Image:1i78.png|left|200px]]


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{{STRUCTURE_1i78|  PDB=1i78  |  SCENE=  }}  
{{STRUCTURE_1i78|  PDB=1i78  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF OUTER MEMBRANE PROTEASE OMPT FROM ESCHERICHIA COLI'''
===CRYSTAL STRUCTURE OF OUTER MEMBRANE PROTEASE OMPT FROM ESCHERICHIA COLI===




==Overview==
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OmpT from Escherichia coli belongs to a family of highly homologous outer membrane proteases, known as omptins, which are implicated in the virulence of several pathogenic Gram-negative bacteria. Here we present the crystal structure of OmpT, which shows a 10-stranded antiparallel beta-barrel that protrudes far from the lipid bilayer into the extracellular space. We identified a putative binding site for lipopolysaccharide, a molecule that is essential for OmpT activity. The proteolytic site is located in a groove at the extracellular top of the vase-shaped beta-barrel. Based on the constellation of active site residues, we propose a novel proteolytic mechanism, involving a His-Asp dyad and an Asp-Asp couple that activate a putative nucleophilic water molecule. The active site is fully conserved within the omptin family. Therefore, the structure described here provides a sound basis for the design of drugs against omptin-mediated bacterial pathogenesis. Coordinates are in the Protein Data Bank (accession No. 1I78)
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{{ABSTRACT_PUBMED_11566868}}


==About this Structure==
==About this Structure==
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[[Category: Integral outer membrane protein]]
[[Category: Integral outer membrane protein]]
[[Category: Protease]]
[[Category: Protease]]
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Revision as of 07:31, 1 July 2008

File:1i78.png

Template:STRUCTURE 1i78

CRYSTAL STRUCTURE OF OUTER MEMBRANE PROTEASE OMPT FROM ESCHERICHIA COLI

Template:ABSTRACT PUBMED 11566868

About this Structure

1I78 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site., Vandeputte-Rutten L, Kramer RA, Kroon J, Dekker N, Egmond MR, Gros P, EMBO J. 2001 Sep 17;20(18):5033-9. PMID:11566868

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