2vzv

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(New page: '''Unreleased structure''' The entry 2vzv is ON HOLD Authors: Lammerts van Bueren, A., Ghinet, M.G., Gregg, K., Fleury, A., Brzezinski, R., Boraston, A.B. Description: Substrate Comple...)
Current revision (11:49, 30 March 2022) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 2vzv is ON HOLD
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==Substrate Complex of Amycolatopsis orientalis exo-chitosanase CsxA E541A with chitosan==
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<StructureSection load='2vzv' size='340' side='right'caption='[[2vzv]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2vzv]] is a 2 chain structure with sequence from [https://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=2VZV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VZV FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GCS:D-GLUCOSAMINE'>GCS</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2vzo|2vzo]], [[2vzp|2vzp]], [[2vzq|2vzq]], [[2vzr|2vzr]], [[2vzs|2vzs]], [[2vzt|2vzt]], [[2vzu|2vzu]]</div></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=2vzv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vzv OCA], [https://pdbe.org/2vzv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vzv RCSB], [https://www.ebi.ac.uk/pdbsum/2vzv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vzv ProSAT]</span></td></tr>
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</table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vz/2vzv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2vzv ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Family 2 of the glycoside hydrolase classification is one of the largest families. Structurally characterized members of this family include enzymes with beta-galactosidase activity (Escherichia coli LacZ), beta-glucuronidase activity (Homo sapiens GusB), and beta-mannosidase activity (Bacteroides thetaiotaomicron BtMan2A). Here, we describe the structure of a family 2 glycoside hydrolase, CsxA, from Amycolatopsis orientalis that has exo-beta-D-glucosaminidase (exo-chitosanase) activity. Analysis of a product complex (1.85 A resolution) reveals a unique negatively charged pocket that specifically accommodates the nitrogen of nonreducing end glucosamine residues, allowing this enzyme to discriminate between glucose and glucosamine. This also provides structural evidence for the role of E541 as the catalytic nucleophile and D469 as the catalytic acid/base. The structures of an E541A mutant in complex with a natural beta-1,4-D-glucosamine tetrasaccharide substrate and both E541A and D469A mutants in complex with a pNP-beta-D-glucosaminide synthetic substrate provide insight into interactions in the +1 subsite of this enzyme. Overall, a comparison with the active sites of other GH2 enzymes highlights the unique architecture of the CsxA active site, which imparts specificity for its cationic substrate.
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Authors: Lammerts van Bueren, A., Ghinet, M.G., Gregg, K., Fleury, A., Brzezinski, R., Boraston, A.B.
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The structural basis of substrate recognition in an exo-beta-D-glucosaminidase involved in chitosan hydrolysis.,van Bueren AL, Ghinet MG, Gregg K, Fleury A, Brzezinski R, Boraston AB J Mol Biol. 2009 Jan 9;385(1):131-9. Epub 2008 Oct 19. PMID:18976664<ref>PMID:18976664</ref>
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Description: Substrate Complex of Amycolatopsis orientalis exo-chitosanase CsxA E541A with chitosan
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 13 13:34:44 2008''
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<div class="pdbe-citations 2vzv" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Streptomyces orientalis pittenger and brigham 1956]]
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[[Category: Large Structures]]
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[[Category: Boraston, A B]]
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[[Category: Brzezinski, R]]
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[[Category: Bueren, A Lammerts van]]
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[[Category: Fleury, A]]
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[[Category: Ghinet, M G]]
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[[Category: Gregg, K]]
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[[Category: Chitosan]]
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[[Category: Csxa]]
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[[Category: Exo-beta-d-glucosaminidase]]
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[[Category: Gh2]]
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[[Category: Glycoside hydrolase]]
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[[Category: Hydrolase]]

Current revision

Substrate Complex of Amycolatopsis orientalis exo-chitosanase CsxA E541A with chitosan

PDB ID 2vzv

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