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==Marasmius oreades agglutinin (MOA), papain back.swap W208Q-Q276W variant== | ==Marasmius oreades agglutinin (MOA), papain back.swap W208Q-Q276W variant== | ||
<StructureSection load='6tsn' size='340' side='right'caption='[[6tsn]]' scene=''> | <StructureSection load='6tsn' size='340' side='right'caption='[[6tsn]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TSN OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6tsn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Marasmius_oreades Marasmius oreades]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TSN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TSN FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CZZ:THIARSAHYDROXY-CYSTEINE'>CZZ</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ef2|3ef2]], [[2iho|2iho]]</div></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=6tsn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tsn OCA], [https://pdbe.org/6tsn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tsn RCSB], [https://www.ebi.ac.uk/pdbsum/6tsn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tsn ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Marasmius oreades agglutinin (MOA) is the holotype of an emerging family of fungal chimerolectins and an active Ca(2+)/Mn(2+)-dependent protease, which exhibits a unique papain-like fold with special active site features. Here we investigated the functional significance of the structural elements differentiating MOA from other papain-like cysteine proteases. X-ray crystal structures of MOA co-crystallized with two synthetic substrates reveal cleaved peptides bound to the catalytic site, corresponding to the final products of the proteolytic reaction. Anomalous diffraction data on crystals grown in the presence of calcium and manganese, cadmium or zinc resolve the calcium/manganese preference of MOA and elucidate the inhibitory roles of zinc and cadmium towards papain-like cysteine proteases in general. The reported structures, together with activity data of MOA active site variants, point to a conservation of the general proteolysis mechanism established for papain. Ultimately, the findings suggest that papain and the papain-like domain of MOA are the product of convergent evolution. | |||
Crystal structure of MOA in complex with a peptide fragment: A protease caught in flagranti.,Manna D, Cordara G, Krengel U Curr Res Struct Biol. 2020 Apr 22;2:56-67. doi: 10.1016/j.crstbi.2020.04.003., eCollection 2020. PMID:34235469<ref>PMID:34235469</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6tsn" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Agglutinin 3D structures|Agglutinin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cordara G]] | [[Category: Marasmius oreades]] | ||
[[Category: Krengel U]] | [[Category: Cordara, G]] | ||
[[Category: Manna D]] | [[Category: Krengel, U]] | ||
[[Category: Manna, D]] | |||
[[Category: Calcium-binding protein]] | |||
[[Category: Fungal chimerolectin]] | |||
[[Category: Manganese-binding protein]] | |||
[[Category: Papain-like cysteine protease]] | |||
[[Category: Protease-substrate complex]] | |||
[[Category: Sugar binding protein]] | |||
[[Category: Toxin]] | |||
Revision as of 12:06, 21 July 2021
Marasmius oreades agglutinin (MOA), papain back.swap W208Q-Q276W variantMarasmius oreades agglutinin (MOA), papain back.swap W208Q-Q276W variant
Structural highlights
Publication Abstract from PubMedThe Marasmius oreades agglutinin (MOA) is the holotype of an emerging family of fungal chimerolectins and an active Ca(2+)/Mn(2+)-dependent protease, which exhibits a unique papain-like fold with special active site features. Here we investigated the functional significance of the structural elements differentiating MOA from other papain-like cysteine proteases. X-ray crystal structures of MOA co-crystallized with two synthetic substrates reveal cleaved peptides bound to the catalytic site, corresponding to the final products of the proteolytic reaction. Anomalous diffraction data on crystals grown in the presence of calcium and manganese, cadmium or zinc resolve the calcium/manganese preference of MOA and elucidate the inhibitory roles of zinc and cadmium towards papain-like cysteine proteases in general. The reported structures, together with activity data of MOA active site variants, point to a conservation of the general proteolysis mechanism established for papain. Ultimately, the findings suggest that papain and the papain-like domain of MOA are the product of convergent evolution. Crystal structure of MOA in complex with a peptide fragment: A protease caught in flagranti.,Manna D, Cordara G, Krengel U Curr Res Struct Biol. 2020 Apr 22;2:56-67. doi: 10.1016/j.crstbi.2020.04.003., eCollection 2020. PMID:34235469[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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