1i78

<table><tr><td colspan='2'>[[1i78]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I78 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I78 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OMPT ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Omptin Omptin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.49 3.4.23.49] </span></td></tr>

[[https://www.uniprot.org/uniprot/OMPT_ECOLI OMPT_ECOLI]] Protease that can cleave T7 RNA polymerase, ferric enterobactin receptor protein (FEP), antimicrobial peptide protamine and other proteins. This protease has a specificity for paired basic residues.<ref>PMID:9683502</ref>

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== Publication Abstract from PubMed ==

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)

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<ref>PMID:11566868</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1i78" style="background-color:#fffaf0;"></div>

[[Category: Ecoli]]

[[Category: Dekker, N]]

[[Category: Egmond, M R]]

[[Category: Gros, P]]

[[Category: Kramer, R A]]

[[Category: Kroon, J]]

[[Category: Vandeputte-Rutten, L]]

[[Category: Protease]]