2vzv

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[[Image:2vzv.png|left|200px]]
 
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==Substrate Complex of Amycolatopsis orientalis exo-chitosanase CsxA E541A with chitosan==
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The line below this paragraph, containing "STRUCTURE_2vzv", creates the "Structure Box" on the page.
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<StructureSection load='2vzv' size='340' side='right'caption='[[2vzv]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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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{{STRUCTURE_2vzv| PDB=2vzv | SCENE= }}
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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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===SUBSTRATE COMPLEX OF AMYCOLATOPSIS ORIENTALIS EXO-CHITOSANASE CSXA E541A WITH CHITOSAN===
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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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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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The line below this paragraph, {{ABSTRACT_PUBMED_18976664}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2vzv" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18976664 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18976664}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Streptomyces orientalis pittenger and brigham 1956]]
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[[2vzv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Amycolatopsis_orientalis Amycolatopsis orientalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VZV OCA].
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[[Category: Large Structures]]
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[[Category: Boraston, A B]]
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==Reference==
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[[Category: Brzezinski, R]]
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<ref group="xtra">PMID:018976664</ref><references group="xtra"/>
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[[Category: Bueren, A Lammerts van]]
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[[Category: Amycolatopsis orientalis]]
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[[Category: Fleury, A]]
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[[Category: Boraston, A B.]]
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[[Category: Ghinet, M G]]
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[[Category: Brzezinski, R.]]
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[[Category: Gregg, K]]
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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]]
[[Category: Chitosan]]
[[Category: Csxa]]
[[Category: Csxa]]

Current revision

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

PDB ID 2vzv

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