View source for 9pks


==The structure of O-glycopeptidase BcM60F from Bacteroides caccae==
<StructureSection load='9pks' size='340' side='right'caption='[[9pks]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9pks]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_caccae_ATCC_43185 Bacteroides caccae ATCC 43185]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9PKS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9PKS 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=9pks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9pks OCA], [https://pdbe.org/9pks PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9pks RCSB], [https://www.ebi.ac.uk/pdbsum/9pks PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9pks ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A413IVK2_9BACE A0A413IVK2_9BACE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
O-glycopeptidases are enzymes that hydrolyze the peptide bonds in glycoproteins by a mechanism that involves specific recognition of O-linked glycans on the substrate. Bacteroides caccae, an accomplished mucin degrader, is a member of the human gut microbiota with sixteen genes encoding putative O-glycopeptidases in the peptidase_M60 family. At present, the diversity of substrate selectivity in O-glycopeptidases is not well-understood nor is the rationale behind their expansion in bacteria such as B. caccae. Here we reveal the activity and diversity of the peptidase_M60 O-glycopeptidases encoded in the B. caccae genome. At least thirteen of the sixteen peptidase_M60 genes encode active mucinolytic enzymes. Targeted functional studies by a high-throughput FRET screen combined with detailed kinetic analyses reveal that five examples in an uncharacterized clade of peptidase_M60 proteins are specifically O-glycopeptidases with different substrate selectivities despite their relatively high degree of relatedness. Structural analyses of these enzymes, including bound complexes, reveal new insight into the molecular underpinnings of O-glycopeptidase diversity. This highlights the larger context of how varied the selectivity of peptidase_M60 O-glycopeptidases can be for the glycan moiety and/or the peptide portion of the substrates, and why mucin degraders like B. caccae diversify O-glycopeptidase substrate repertoires to potentially maximize breakdown of this extraordinarily complex polymer.

Substrate recognition and cleavage by mucin degrading O-glycopeptidases from the gut microbe Bacteroides caccae.,Pluvinage B, Bourdon K, Canil O, Deventer A, Alvarez B, Mihalynuk L, Thompson N, Wakarchuk W, Boraston AB J Biol Chem. 2026 Jun 4:113222. doi: 10.1016/j.jbc.2026.113222. PMID:42248462<ref>PMID:42248462</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9pks" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bacteroides caccae ATCC 43185]]
[[Category: Large Structures]]
[[Category: Boraston AB]]
[[Category: Pluvinage B]]