1i78
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1i78.jpg|left|200px]] | [[Image:1i78.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1i78", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{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''' | ||
| Line 32: | Line 29: | ||
[[Category: Kroon, J.]] | [[Category: Kroon, J.]] | ||
[[Category: Vandeputte-Rutten, L.]] | [[Category: Vandeputte-Rutten, L.]] | ||
| - | [[Category: | + | [[Category: Beta barrel]] |
| - | [[Category: | + | [[Category: Integral outer membrane protein]] |
| - | [[Category: | + | [[Category: Protease]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:39:30 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 16:39, 2 May 2008
CRYSTAL STRUCTURE OF OUTER MEMBRANE PROTEASE OMPT FROM ESCHERICHIA COLI
Overview
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)
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 Page seeded by OCA on Fri May 2 19:39:30 2008
