5fnx: Difference between revisions
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==Crystal structure at pH 9.0 of a potato STI-Kunitz bi-functional inhibitor of serine and aspartic proteases in space group p4322 and ph 9.0== | ==Crystal structure at pH 9.0 of a potato STI-Kunitz bi-functional inhibitor of serine and aspartic proteases in space group p4322 and ph 9.0== | ||
<StructureSection load='5fnx' size='340' side='right' caption='[[5fnx]], [[Resolution|resolution]] 2.65Å' scene=''> | <StructureSection load='5fnx' size='340' side='right'caption='[[5fnx]], [[Resolution|resolution]] 2.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5fnx]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FNX OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5fnx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Potato Potato]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FNX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FNX FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fnw|5fnw]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fnw|5fnw]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5fnx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fnx OCA], [http://pdbe.org/5fnx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fnx RCSB], [http://www.ebi.ac.uk/pdbsum/5fnx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fnx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Potato]] | |||
[[Category: Guerra, Y]] | [[Category: Guerra, Y]] | ||
[[Category: Rudino-Pinera, E]] | [[Category: Rudino-Pinera, E]] | ||
Revision as of 10:27, 6 May 2020
Crystal structure at pH 9.0 of a potato STI-Kunitz bi-functional inhibitor of serine and aspartic proteases in space group p4322 and ph 9.0Crystal structure at pH 9.0 of a potato STI-Kunitz bi-functional inhibitor of serine and aspartic proteases in space group p4322 and ph 9.0
Structural highlights
Publication Abstract from PubMedBi-functional inhibitors from the Kunitz-type soybean trypsin inhibitor (STI) family are glycosylated proteins able to inhibit serine and aspartic proteases. Here we report six crystal structures of the wild-type and a non-glycosylated mutant of the bifunctional inhibitor E3Ad obtained at different pH values and space groups. The crystal structures show that E3Ad adopts the typical beta-trefoil fold of the STI family exhibiting some conformational changes due to pH variations and crystal packing. Despite the high sequence identity with a recently reported potato cathepsin D inhibitor (PDI), three-dimensional structures obtained in this work show a significant conformational change in the protease-binding loop proposed for aspartic protease inhibition. The E3Ad binding loop for serine protease inhibition is also proposed, based on structural similarity with a novel non-canonical conformation described for the double-headed inhibitor API-A from the Kunitz-type STI family. In addition, structural and sequence analyses suggest that bifunctional inhibitors of serine and aspartic proteases from the Kunitz-type STI family are more similar to double-headed inhibitor API-A than other inhibitors with a canonical protease-binding loop. Structures of a bi-functional Kunitz-type STI family inhibitor of serine and aspartic proteases: Could the aspartic protease inhibition have evolved from a canonical serine protease-binding loop?,Guerra Y, Valiente PA, Pons T, Berry C, Rudino-Pinera E J Struct Biol. 2016 Aug;195(2):259-71. doi: 10.1016/j.jsb.2016.06.014. Epub 2016 , Jun 18. PMID:27329566[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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