5mu9
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==MOA-E-64 complex== | |
| + | <StructureSection load='5mu9' size='340' side='right' caption='[[5mu9]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5mu9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MU9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MU9 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ef2|3ef2]], [[2iho|2iho]], [[5d61|5d61]], [[5d62|5d62]], [[5d63|5d63]]</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=5mu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mu9 OCA], [http://pdbe.org/5mu9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mu9 RCSB], [http://www.ebi.ac.uk/pdbsum/5mu9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mu9 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | An important function of fungal lectins is to protect their host. Marasmius oreades agglutinin (MOA) is toxic to nematodes and exerts its protective effect through protease activity. Its proteolytic function is associated with a papain-like dimerization domain. The closest homologue of MOA is Polyporus squamosus lectin 1a (PSL1a). Here, we probed PSL1a for catalytic activity and confirmed that it is a calcium-dependent cysteine protease, like MOA. The X-ray crystal structures of PSL1a (1.5 A) and MOA (1.3 A) in complex with calcium and the irreversible cysteine protease inhibitor E-64 elucidated the structural basis for their mechanism of action. The comparison with other calcium-dependent proteases (calpains, LapG) reveals a unique metal-dependent activation mechanism relying on a calcium-induced backbone shift and intradimer cooperation. Intriguingly, the enzymes appear to use a tyrosine-gating mechanism instead of pro-peptide processing. A search for potential MOA orthologues suggests the existence of a whole new family of fungal chimerolectins with these unique features. | ||
| - | + | Family of Papain-Like Fungal Chimerolectins with Distinct Ca2+-Dependent Activation Mechanism.,Cordara G, Manna D, Krengel U Biochemistry. 2017 Aug 22. doi: 10.1021/acs.biochem.7b00317. PMID:28665586<ref>PMID:28665586</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5mu9" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Cordara, G]] | ||
[[Category: Krengel, U]] | [[Category: Krengel, U]] | ||
[[Category: Manna, D]] | [[Category: Manna, D]] | ||
| - | [[Category: | + | [[Category: Calcium-binding]] |
| + | [[Category: E-64 inhibitor complex]] | ||
| + | [[Category: Lectin]] | ||
| + | [[Category: Papain-like protease]] | ||
| + | [[Category: Sugar binding protein]] | ||
Revision as of 04:18, 30 August 2017
MOA-E-64 complex
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