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| | <StructureSection load='2w1n' size='340' side='right'caption='[[2w1n]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='2w1n' size='340' side='right'caption='[[2w1n]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2w1n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_perfringens"_veillon_and_zuber_1898 "bacillus perfringens" veillon and zuber 1898]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W1N OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2W1N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2w1n]] 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=2W1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W1N FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2cbi|2cbi]], [[2j1e|2j1e]], [[2j7m|2j7m]], [[2j1a|2j1a]], [[2cbj|2cbj]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </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=2w1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w1n OCA], [https://pdbe.org/2w1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w1n RCSB], [https://www.ebi.ac.uk/pdbsum/2w1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w1n ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2w1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w1n OCA], [http://pdbe.org/2w1n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2w1n RCSB], [http://www.ebi.ac.uk/pdbsum/2w1n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2w1n ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/OGA_CLOP1 OGA_CLOP1] Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | *[[Beta-Hexosaminidase|Beta-Hexosaminidase]] | | *[[Beta-Hexosaminidase|Beta-Hexosaminidase]] |
| | *[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]] | | *[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]] |
| | + | *[[O-GlcNAcase|O-GlcNAcase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus perfringens veillon and zuber 1898]] | + | [[Category: Clostridium perfringens]] |
| - | [[Category: Beta-N-acetylhexosaminidase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Adams, J J]] | + | [[Category: Adams JJ]] |
| - | [[Category: Boraston, A B]] | + | [[Category: Boraston AB]] |
| - | [[Category: Czjzek, M]] | + | [[Category: Czjzek M]] |
| - | [[Category: Ficko-Blean, E]] | + | [[Category: Ficko-Blean E]] |
| - | [[Category: Gregg, K J]] | + | [[Category: Gregg KJ]] |
| - | [[Category: Hehemann, J H]] | + | [[Category: Hehemann JH]] |
| - | [[Category: Smith, S J]] | + | [[Category: Smith SJ]] |
| - | [[Category: Beta-n-acetylglucosaminidase]]
| + | |
| - | [[Category: Clostridium perfringen]]
| + | |
| - | [[Category: Cohesin]]
| + | |
| - | [[Category: Coiled coil]]
| + | |
| - | [[Category: Fibronectin type-iii]]
| + | |
| - | [[Category: Glycosidase]]
| + | |
| - | [[Category: Glycoside hydrolase]]
| + | |
| - | [[Category: Hexosaminidase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
OGA_CLOP1 Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Common features of the extracellular carbohydrate-active virulence factors involved in host-pathogen interactions are their large sizes and modular complexities. This has made them recalcitrant to structural analysis, and therefore our understanding of the significance of modularity in these important proteins is lagging. Clostridium perfringens is a prevalent human pathogen that harbors a wide array of large, extracellular carbohydrate-active enzymes and is an excellent and relevant model system to approach this problem. Here we describe the complete structure of C. perfringens GH84C (NagJ), a 1001-amino acid multimodular homolog of the C. perfringens micro-toxin, which was determined using a combination of small angle x-ray scattering and x-ray crystallography. The resulting structure reveals unprecedented insight into how catalysis, carbohydrate-specific adherence, and the formation of molecular complexes with other enzymes via an ultra-tight protein-protein interaction are spatially coordinated in an enzyme involved in a host-pathogen interaction.
Portrait of an enzyme, a complete structural analysis of a multimodular {beta}-N-acetylglucosaminidase from Clostridium perfringens.,Ficko-Blean E, Gregg KJ, Adams JJ, Hehemann JH, Czjzek M, Smith SP, Boraston AB J Biol Chem. 2009 Apr 10;284(15):9876-84. Epub 2009 Feb 4. PMID:19193644[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ficko-Blean E, Gregg KJ, Adams JJ, Hehemann JH, Czjzek M, Smith SP, Boraston AB. Portrait of an enzyme, a complete structural analysis of a multimodular {beta}-N-acetylglucosaminidase from Clostridium perfringens. J Biol Chem. 2009 Apr 10;284(15):9876-84. Epub 2009 Feb 4. PMID:19193644 doi:10.1074/jbc.M808954200
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