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2vzt
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2vzt is ON HOLD Authors: Lammerts van Bueren, A., Ghinet, M.G., Gregg, K., Fleury, A., Brzezinski, R., Boraston, A.B. Description: Complex of Amyco...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Complex of Amycolatopsis orientalis exo-chitosanase CsxA E541A with PNP-beta-D-glucosamine== | |
| + | <StructureSection load='2vzt' size='340' side='right'caption='[[2vzt]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2vzt]] 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=2VZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VZT 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>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=PNJ:PNP-BETA-D-GLUCOSAMINE'>PNJ</scene></td></tr> | ||
| + | <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]], [[2vzu|2vzu]], [[2vzv|2vzv]]</div></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=2vzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vzt OCA], [https://pdbe.org/2vzt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vzt RCSB], [https://www.ebi.ac.uk/pdbsum/2vzt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vzt ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vz/2vzt_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=2vzt ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2vzt" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Streptomyces orientalis pittenger and brigham 1956]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Boraston, A B]] | ||
| + | [[Category: Brzezinski, R]] | ||
| + | [[Category: Bueren, A Lammerts van]] | ||
| + | [[Category: Fleury, A]] | ||
| + | [[Category: Ghinet, M G]] | ||
| + | [[Category: Gregg, K]] | ||
| + | [[Category: Csxa]] | ||
| + | [[Category: Exo-beta-d-glucosaminidase]] | ||
| + | [[Category: Gh2]] | ||
| + | [[Category: Glycoside hydrolase]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Pnp-glucosamine]] | ||
Current revision
Complex of Amycolatopsis orientalis exo-chitosanase CsxA E541A with PNP-beta-D-glucosamine
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