1wkr

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(New page: 200px<br /><applet load="1wkr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wkr, resolution 1.30&Aring;" /> '''Crystal structure of...)
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[[Image:1wkr.gif|left|200px]]<br /><applet load="1wkr" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1wkr, resolution 1.30&Aring;" />
 
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'''Crystal structure of aspartic proteinase from Irpex lacteus'''<br />
 
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==Overview==
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==Crystal structure of aspartic proteinase from Irpex lacteus==
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The crystal structure of Irpex lacteus aspartic proteinase (ILAP) in, complex with pepstatin (a six amino acid residue peptide-like inhibitor), was determined at 1.3A resolution. ILAP is a pepsin-like enzyme, widely, distributed in nature, with high milk-clotting activity relative to, proteolytic activity. The overall structure was in good topological, agreement with pepsin and other aspartic proteases. The structure and, interaction pattern around the catalytic site were conserved, in agreement, with the other aspartic proteinase/inhibitor complex structures reported, previously. The high-resolution data also supported the transition state, model, as proposed previously for the catalytic mechanism of aspartic, proteinase. Unlike the other aspartic proteinases, ILAP was found to, require hydrophobic residues either in the P(1) or P(1') site, and also in, the P(4) and/or P(3) site(s) for secondary interactions. The inhibitor, complex structure also revealed the substrate binding mechanism of ILAP at, the P(3) and P(4) site of the substrate, where the inserted loop built up, the unique hydrophobic pocket at the P(4) site.
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<StructureSection load='1wkr' size='340' side='right'caption='[[1wkr]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1wkr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Irpex_lacteus Irpex lacteus] and [https://en.wikipedia.org/wiki/Streptomyces_argenteolus_subsp._toyonakensis Streptomyces argenteolus subsp. toyonakensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WKR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WKR FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IVA:ISOVALERIC+ACID'>IVA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=STA:STATINE'>STA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wkr OCA], [https://pdbe.org/1wkr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wkr RCSB], [https://www.ebi.ac.uk/pdbsum/1wkr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wkr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CARP_IRPLA CARP_IRPLA]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wk/1wkr_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1wkr ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystal structure of Irpex lacteus aspartic proteinase (ILAP) in complex with pepstatin (a six amino acid residue peptide-like inhibitor) was determined at 1.3A resolution. ILAP is a pepsin-like enzyme, widely distributed in nature, with high milk-clotting activity relative to proteolytic activity. The overall structure was in good topological agreement with pepsin and other aspartic proteases. The structure and interaction pattern around the catalytic site were conserved, in agreement with the other aspartic proteinase/inhibitor complex structures reported previously. The high-resolution data also supported the transition state model, as proposed previously for the catalytic mechanism of aspartic proteinase. Unlike the other aspartic proteinases, ILAP was found to require hydrophobic residues either in the P(1) or P(1') site, and also in the P(4) and/or P(3) site(s) for secondary interactions. The inhibitor complex structure also revealed the substrate binding mechanism of ILAP at the P(3) and P(4) site of the substrate, where the inserted loop built up the unique hydrophobic pocket at the P(4) site.
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==About this Structure==
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Crystal structure of aspartic proteinase from Irpex lacteus in complex with inhibitor pepstatin.,Fujimoto Z, Fujii Y, Kaneko S, Kobayashi H, Mizuno H J Mol Biol. 2004 Aug 27;341(5):1227-35. PMID:15321718<ref>PMID:15321718</ref>
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1WKR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Irpex_lacteus Irpex lacteus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Polyporopepsin Polyporopepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.29 3.4.23.29] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WKR OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of aspartic proteinase from Irpex lacteus in complex with inhibitor pepstatin., Fujimoto Z, Fujii Y, Kaneko S, Kobayashi H, Mizuno H, J Mol Biol. 2004 Aug 27;341(5):1227-35. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15321718 15321718]
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</div>
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[[Category: Irpex lacteus]]
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<div class="pdbe-citations 1wkr" style="background-color:#fffaf0;"></div>
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[[Category: Polyporopepsin]]
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[[Category: Single protein]]
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[[Category: Fujii, Y.]]
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[[Category: Fujimoto, Z.]]
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[[Category: Kaneko, S.]]
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[[Category: Kobayashi, H.]]
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[[Category: Mizuno, H.]]
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[[Category: SO4]]
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[[Category: enzyme-inhibitor complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:29:51 2007''
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==See Also==
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*[[Pepsin|Pepsin]]
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*[[Proteinase 3D structures|Proteinase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Irpex lacteus]]
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[[Category: Large Structures]]
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[[Category: Streptomyces argenteolus subsp. toyonakensis]]
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[[Category: Fujii Y]]
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[[Category: Fujimoto Z]]
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[[Category: Kaneko S]]
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[[Category: Kobayashi H]]
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[[Category: Mizuno H]]

Current revision

Crystal structure of aspartic proteinase from Irpex lacteus

PDB ID 1wkr

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