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1i78

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[[Image:1i78.jpg|left|200px]]<br /><applet load="1i78" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1i78.jpg|left|200px]]
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caption="1i78, resolution 2.6&Aring;" />
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'''CRYSTAL STRUCTURE OF OUTER MEMBRANE PROTEASE OMPT FROM ESCHERICHIA COLI'''<br />
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{{Structure
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|PDB= 1i78 |SIZE=350|CAPTION= <scene name='initialview01'>1i78</scene>, resolution 2.6&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene> and <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>
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|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]
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|GENE= OMPT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''CRYSTAL STRUCTURE OF OUTER MEMBRANE PROTEASE OMPT FROM ESCHERICHIA COLI'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1I78 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=BOG:'>BOG</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I78 OCA].
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1I78 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I78 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11566868 11566868]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11566868 11566868]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Omptin]]
[[Category: Omptin]]
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[[Category: protease]]
[[Category: protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:08:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:46:34 2008''

Revision as of 09:46, 20 March 2008


PDB ID 1i78

Drag the structure with the mouse to rotate
, resolution 2.6Å
Ligands: and
Gene: OMPT (Escherichia coli)
Activity: Omptin, with EC number 3.4.23.49
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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