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[[Image:1wkr.gif|left|200px]]
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{{STRUCTURE_1wkr|  PDB=1wkr  |  SCENE=  }}
'''Crystal structure of aspartic proteinase from Irpex lacteus'''


==Crystal structure of aspartic proteinase from Irpex lacteus==
<StructureSection load='1wkr' size='340' side='right'caption='[[1wkr]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CARP_IRPLA CARP_IRPLA]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wk/1wkr_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1WKR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Irpex_lacteus Irpex lacteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WKR OCA].
</div>
<div class="pdbe-citations 1wkr" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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://www.ncbi.nlm.nih.gov/pubmed/15321718 15321718]
*[[Pepsin|Pepsin]]
*[[Proteinase 3D structures|Proteinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Irpex lacteus]]
[[Category: Irpex lacteus]]
[[Category: Polyporopepsin]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Streptomyces argenteolus subsp. toyonakensis]]
[[Category: Fujii, Y.]]
[[Category: Fujii Y]]
[[Category: Fujimoto, Z.]]
[[Category: Fujimoto Z]]
[[Category: Kaneko, S.]]
[[Category: Kaneko S]]
[[Category: Kobayashi, H.]]
[[Category: Kobayashi H]]
[[Category: Mizuno, H.]]
[[Category: Mizuno H]]
[[Category: Enzyme-inhibitor complex]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 13:48:58 2008''

Latest revision as of 04:59, 17 October 2024

Crystal structure of aspartic proteinase from Irpex lacteus

1wkr, resolution 1.30Å

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