7js4
From Proteopedia
(Difference between revisions)
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==The structure of the M60 catalytic domain with the CBM51-1 and CBM51-2 domains from Clostridium perfringens ZmpB== | ==The structure of the M60 catalytic domain with the CBM51-1 and CBM51-2 domains from Clostridium perfringens ZmpB== | ||
| - | <StructureSection load='7js4' size='340' side='right'caption='[[7js4]]' scene=''> | + | <StructureSection load='7js4' size='340' side='right'caption='[[7js4]], [[Resolution|resolution]] 4.60Å' 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=7JS4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JS4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7js4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clop1 Clop1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JS4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JS4 FirstGlance]. <br> |
| - | </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=7js4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7js4 OCA], [https://pdbe.org/7js4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7js4 RCSB], [https://www.ebi.ac.uk/pdbsum/7js4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7js4 ProSAT]</span></td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CPF_1489 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=195103 CLOP1])</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=7js4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7js4 OCA], [https://pdbe.org/7js4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7js4 RCSB], [https://www.ebi.ac.uk/pdbsum/7js4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7js4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A challenge faced by peptidases is the recognition of highly diverse substrates. A feature of some peptidase families is the capacity to specifically use post-translationally added glycans present on their protein substrates as a recognition determinant. This is ultimately critical to enabling peptide bond hydrolysis. This class of enzyme is also frequently large and architecturally sophisticated. However, the molecular details underpinning glycan recognition by these O-glycopeptidases, the importance of these interactions, and the functional roles of their ancillary domains remain unclear. Here, using the Clostridium perfringens ZmpA, ZmpB, and ZmpC M60 peptidases as model proteins, we provide structural and functional insight into how these intricate proteins recognize glycans as part of catalytic and noncatalytic substrate recognition. Structural, kinetic, and mutagenic analyses support the key role of glycan recognition within the M60 domain catalytic site, though they point to ZmpA as an apparently inactive enzyme. Wider examination of the Zmp domain content reveals noncatalytic carbohydrate binding as a feature of these proteins. The complete three-dimensional structure of ZmpB provides rare insight into the overall molecular organization of a highly multimodular enzyme and reveals how the interplay of individual domain function may influence biological activity. O-glycopeptidases frequently occur in host-adapted microbes that inhabit or attack mucus layers. Therefore, we anticipate that these results will be fundamental to informing more detailed models of how the glycoproteins that are abundant in mucus are destroyed as part of pathogenic processes or liberated as energy sources during normal commensal lifestyles. | ||
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| + | Architecturally complex O-glycopeptidases are customized for mucin recognition and hydrolysis.,Pluvinage B, Ficko-Blean E, Noach I, Stuart C, Thompson N, McClure H, Buenbrazo N, Wakarchuk W, Boraston AB Proc Natl Acad Sci U S A. 2021 Mar 9;118(10). pii: 2019220118. doi:, 10.1073/pnas.2019220118. PMID:33658366<ref>PMID:33658366</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7js4" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Clop1]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Boraston | + | [[Category: Boraston, A B]] |
| - | [[Category: Pluvinage B]] | + | [[Category: Pluvinage, B]] |
| + | [[Category: Glycopeptidase]] | ||
| + | [[Category: Hydrolase]] | ||
Revision as of 06:18, 18 August 2021
The structure of the M60 catalytic domain with the CBM51-1 and CBM51-2 domains from Clostridium perfringens ZmpB
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