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| | <StructureSection load='2x09' size='340' side='right'caption='[[2x09]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='2x09' size='340' side='right'caption='[[2x09]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2x09]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptomyces_orientalis"_pittenger_and_brigham_1956 "streptomyces orientalis" pittenger and brigham 1956]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X09 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2X09 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2x09]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Amycolatopsis_orientalis Amycolatopsis orientalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X09 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=X09:AMINO-AUSTRALINE'>X09</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]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2x05|2x05]], [[2vzr|2vzr]], [[2vzu|2vzu]], [[2vzs|2vzs]], [[2vzt|2vzt]], [[2vzo|2vzo]], [[2vzq|2vzq]], [[2vzp|2vzp]], [[2vzv|2vzv]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=X09:AMINO-AUSTRALINE'>X09</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exo-1,4-beta-D-glucosaminidase Exo-1,4-beta-D-glucosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.165 3.2.1.165] </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=2x09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x09 OCA], [https://pdbe.org/2x09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x09 RCSB], [https://www.ebi.ac.uk/pdbsum/2x09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x09 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=2x09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x09 OCA], [http://pdbe.org/2x09 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x09 RCSB], [http://www.ebi.ac.uk/pdbsum/2x09 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x09 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/EBDG_AMYOR EBDG_AMYOR] Hydrolyzes chitosan and chitooligosaccharides with retention of anomeric configuration. Has maximum activity on chitotetraose, chitopentaose and their corresponding alcohols, with a slight decrease in the rate of hydrolysis on longer chains. Has no activity against beta-D-glucopyranoside, beta-D-xylopyranoside, beta-D-mannoside, beta-D-glucuronide, beta-D-galactoside, beta-D-N-acetylgalactosamide, beta-D-N-acetylglucosaminide and alpha-D-N-acetylglucosaminide.<ref>PMID:16316314</ref> <ref>PMID:2351651</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Streptomyces orientalis pittenger and brigham 1956]] | + | [[Category: Amycolatopsis orientalis]] |
| - | [[Category: Exo-1,4-beta-D-glucosaminidase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Boraston, A B]] | + | [[Category: Boraston AB]] |
| - | [[Category: Brzezinski, R]] | + | [[Category: Brzezinski R]] |
| - | [[Category: Ghinet, M G]] | + | [[Category: Ghinet MG]] |
| - | [[Category: Pluvinage, B]] | + | [[Category: Pluvinage B]] |
| - | [[Category: Stubbs, K A]] | + | [[Category: Stubbs KA]] |
| - | [[Category: Csxa]]
| + | |
| - | [[Category: Exo-beta-d-glucosaminidase]]
| + | |
| - | [[Category: Gh2]]
| + | |
| - | [[Category: Glycosidase]]
| + | |
| - | [[Category: Glycoside hydrolase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
EBDG_AMYOR Hydrolyzes chitosan and chitooligosaccharides with retention of anomeric configuration. Has maximum activity on chitotetraose, chitopentaose and their corresponding alcohols, with a slight decrease in the rate of hydrolysis on longer chains. Has no activity against beta-D-glucopyranoside, beta-D-xylopyranoside, beta-D-mannoside, beta-D-glucuronide, beta-D-galactoside, beta-D-N-acetylgalactosamide, beta-D-N-acetylglucosaminide and alpha-D-N-acetylglucosaminide.[1] [2]
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
The synthesis of amino-derivatives of castanospermine and australine and their characterisation as inhibitors of the exo-beta-D-glucosaminidase CsxA through enzyme kinetics and X-ray structural analysis is described.
Inhibition of the exo-beta-D-glucosaminidase CsxA by a glucosamine-configured castanospermine and an amino-australine analogue.,Pluvinage B, Ghinet MG, Brzezinski R, Boraston AB, Stubbs KA Org Biomol Chem. 2009 Oct 21;7(20):4169-72. Epub 2009 Aug 14. PMID:19795054[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cote N, Fleury A, Dumont-Blanchette E, Fukamizo T, Mitsutomi M, Brzezinski R. Two exo-beta-D-glucosaminidases/exochitosanases from actinomycetes define a new subfamily within family 2 of glycoside hydrolases. Biochem J. 2006 Mar 15;394(Pt 3):675-86. PMID:16316314 doi:http://dx.doi.org/10.1042/BJ20051436
- ↑ Nanjo F, Katsumi R, Sakai K. Purification and characterization of an exo-beta-D-glucosaminidase, a novel type of enzyme, from Nocardia orientalis. J Biol Chem. 1990 Jun 15;265(17):10088-94. PMID:2351651
- ↑ Pluvinage B, Ghinet MG, Brzezinski R, Boraston AB, Stubbs KA. Inhibition of the exo-beta-D-glucosaminidase CsxA by a glucosamine-configured castanospermine and an amino-australine analogue. Org Biomol Chem. 2009 Oct 21;7(20):4169-72. Epub 2009 Aug 14. PMID:19795054 doi:10.1039/b913235j
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