4lp9
From Proteopedia
(Difference between revisions)
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| - | + | ==Endothiapepsin complexed with Phe-reduced-Tyr peptide.== | |
| - | ===Endothiapepsin | + | <StructureSection load='4lp9' size='340' side='right' caption='[[4lp9]], [[Resolution|resolution]] 1.35Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4lp9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cryphonectria_parasitica Cryphonectria parasitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LP9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LP9 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=22G:N-[(2S)-2-AMINO-3-PHENYLPROPYL]-L-TYROSINE'>22G</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gvx|1gvx]], [[1gvt|1gvt]], [[1gvu|1gvu]], [[1gvv|1gvv]], [[1gvw|1gvw]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endothiapepsin Endothiapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.22 3.4.23.22] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lp9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lp9 RCSB], [http://www.ebi.ac.uk/pdbsum/4lp9 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Endothiapepsin is a typical member of the aspartic proteinase family. The catalytic mechanism of this family is attributed to two conserved catalytic aspartate residues, which coordinate the hydrolysis of a peptide bond. An oligopeptide inhibitor (IC50 = 0.62 microM) based on a reduced-bond transition-state inhibitor of mucorpepsin was co-crystallized with endothiapepsin and the crystal structure of the enzyme-inhibitor complex was determined at 1.35 A resolution. A total of 12 hydrogen bonds between the inhibitor and the active-site residues were identified. The resulting structure demonstrates a number of novel subsite interactions in the active-site cleft. | ||
| - | + | The structure of endothiapepsin complexed with a Phe-Tyr reduced-bond inhibitor at 1.35 A resolution.,Guo J, Cooper JB, Wood SP Acta Crystallogr F Struct Biol Commun. 2014 Jan;70(Pt 1):30-3. doi:, 10.1107/S2053230X13032974. Epub 2013 Dec 24. PMID:24419612<ref>PMID:24419612</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Cryphonectria parasitica]] | [[Category: Cryphonectria parasitica]] | ||
[[Category: Endothiapepsin]] | [[Category: Endothiapepsin]] | ||
| - | [[Category: Cooper, J B | + | [[Category: Cooper, J B]] |
| - | [[Category: Guo, J | + | [[Category: Guo, J]] |
| - | [[Category: Wood, S P | + | [[Category: Wood, S P]] |
[[Category: Aspartic proteinase fold]] | [[Category: Aspartic proteinase fold]] | ||
[[Category: Hydrolase-hydrolase inhibitor complex]] | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
[[Category: Proteolysis]] | [[Category: Proteolysis]] | ||
Revision as of 18:22, 21 December 2014
Endothiapepsin complexed with Phe-reduced-Tyr peptide.
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