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5kd2

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==BT_4244 metallopeptidase from Bacteroides thetaiotaomicron==
==BT_4244 metallopeptidase from Bacteroides thetaiotaomicron==
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<StructureSection load='5kd2' size='340' side='right' caption='[[5kd2]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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<StructureSection load='5kd2' size='340' side='right'caption='[[5kd2]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5kd2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KD2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KD2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5kd2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron_VPI-5482 Bacteroides thetaiotaomicron VPI-5482]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KD2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KD2 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kd5|5kd5]], [[5kd8|5kd8]], [[5kdj|5kdj]], [[5kdn|5kdn]], [[5kds|5kds]], [[5kdu|5kdu]], [[5kdv|5kdv]], [[5kdw|5kdw]], [[5kdx|5kdx]]</td></tr>
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<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>
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<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=5kd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kd2 OCA], [http://pdbe.org/5kd2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kd2 RCSB], [http://www.ebi.ac.uk/pdbsum/5kd2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kd2 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5kd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kd2 OCA], [https://pdbe.org/5kd2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kd2 RCSB], [https://www.ebi.ac.uk/pdbsum/5kd2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kd2 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q89ZX7_BACTN Q89ZX7_BACTN]
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The vast majority of proteins are posttranslationally altered, with the addition of covalently linked sugars (glycosylation) being one of the most abundant modifications. However, despite the hydrolysis of protein peptide bonds by peptidases being a process essential to all life on Earth, the fundamental details of how peptidases accommodate posttranslational modifications, including glycosylation, has not been addressed. Through biochemical analyses and X-ray crystallographic structures we show that to hydrolyze their substrates, three structurally related metallopeptidases require the specific recognition of O-linked glycan modifications via carbohydrate-specific subsites immediately adjacent to their peptidase catalytic machinery. The three peptidases showed selectivity for different glycans, revealing protein-specific adaptations to particular glycan modifications, yet always cleaved the peptide bond immediately preceding the glycosylated residue. This insight builds upon the paradigm of how peptidases recognize substrates and provides a molecular understanding of glycoprotein degradation.
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Recognition of protein-linked glycans as a determinant of peptidase activity.,Noach I, Ficko-Blean E, Pluvinage B, Stuart C, Jenkins ML, Brochu D, Buenbrazo N, Wakarchuk W, Burke JE, Gilbert M, Boraston AB Proc Natl Acad Sci U S A. 2017 Jan 17. pii: 201615141. doi:, 10.1073/pnas.1615141114. PMID:28096352<ref>PMID:28096352</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5kd2" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Boraston, A B]]
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[[Category: Bacteroides thetaiotaomicron VPI-5482]]
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[[Category: Noach, I]]
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[[Category: Large Structures]]
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[[Category: Hydrolase]]
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[[Category: Boraston AB]]
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[[Category: O-glycopeptidase]]
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[[Category: Noach I]]
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[[Category: Pf13402/m60-like]]
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Current revision

BT_4244 metallopeptidase from Bacteroides thetaiotaomicron

PDB ID 5kd2

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