1i78
From Proteopedia
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|PDB= 1i78 |SIZE=350|CAPTION= <scene name='initialview01'>1i78</scene>, resolution 2.6Å | |PDB= 1i78 |SIZE=350|CAPTION= <scene name='initialview01'>1i78</scene>, resolution 2.6Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene> | + | |LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Omptin Omptin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.49 3.4.23.49] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Omptin Omptin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.49 3.4.23.49] </span> |
|GENE= OMPT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= OMPT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i78 OCA], [http://www.ebi.ac.uk/pdbsum/1i78 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i78 RCSB]</span> | ||
}} | }} | ||
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[[Category: Kroon, J.]] | [[Category: Kroon, J.]] | ||
[[Category: Vandeputte-Rutten, L.]] | [[Category: Vandeputte-Rutten, L.]] | ||
| - | [[Category: BOG]] | ||
| - | [[Category: MPD]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
[[Category: integral outer membrane protein]] | [[Category: integral outer membrane protein]] | ||
[[Category: protease]] | [[Category: protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:15:36 2008'' |
Revision as of 18:15, 30 March 2008
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| , resolution 2.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | OMPT (Escherichia coli) | ||||||
| Activity: | Omptin, with EC number 3.4.23.49 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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