4a4a: Difference between revisions
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<StructureSection load='4a4a' size='340' side='right'caption='[[4a4a]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='4a4a' size='340' side='right'caption='[[4a4a]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4a4a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4a4a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A4A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A4A FirstGlance]. <br> | ||
</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= | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4a4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a4a OCA], [https://pdbe.org/4a4a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a4a RCSB], [https://www.ebi.ac.uk/pdbsum/4a4a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a4a ProSAT]</span></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=4a4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a4a OCA], [https://pdbe.org/4a4a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a4a RCSB], [https://www.ebi.ac.uk/pdbsum/4a4a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a4a ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8XM24_CLOPE Q8XM24_CLOPE] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 23: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Clostridium perfringens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Boraston | [[Category: Boraston AB]] | ||
[[Category: Cid | [[Category: Cid M]] | ||
[[Category: Ficko-Blean | [[Category: Ficko-Blean E]] | ||
[[Category: Stuart | [[Category: Stuart CP]] | ||
[[Category: Suits | [[Category: Suits MD]] | ||
[[Category: Tessier | [[Category: Tessier M]] | ||
[[Category: Woods | [[Category: Woods RJ]] | ||
Latest revision as of 13:46, 9 May 2024
CpGH89 (E483Q, E601Q), from Clostridium perfringens, in complex with its substrate GlcNAc-alpha-1,4-galactoseCpGH89 (E483Q, E601Q), from Clostridium perfringens, in complex with its substrate GlcNAc-alpha-1,4-galactose
Structural highlights
FunctionPublication Abstract from PubMedCpGH89 is a family 89 glycoside hydrolase with exo-alpha-D-N-acetylglucosaminidase activity that is produced by the human and animal pathogen Clostridium perfringens. This enzyme is active on the alpha-D-GlcpNAc-(1 --> 4)-D-Galp motif that is displayed on the class III mucins within the gastric mucosa. Other members of this enzyme family, such as human NAGLU, are active on heparan. A truncated version of CpGH89 was rendered inactive through the mutation of two key catalytic residues, the protein crystallized and its structure determined in complex with alpha-D-GlcpNAc-(1 --> 4)-D-Galp to reveal the molecular details of how this unique disaccharide is recognized by CpGH89. An analysis of this substrate complex not only provides insight into how this enzyme selects for its mucin-presented substrate but also advances our understanding of how its clinically relevant mammalian counterparts are specific for heparan. Structural analysis of a bacterial exo-alpha-D-N-acetylglucosaminidase in complex with an unusual disaccharide found in class III mucin.,Ficko-Blean E, Boraston AB Glycobiology. 2012 May;22(5):590-5. doi: 10.1093/glycob/cwr165. Epub 2011 Nov 16. PMID:22090394[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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