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2w52

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(New page: '''Unreleased structure''' The entry 2w52 is ON HOLD Authors: Vasur, J., Kawai, R., Andersson, E., Igarashi, K., Sandgren, M., Samejima, M., Stahlberg, J. Description: 2 beta-glucans (...)
Current revision (16:42, 3 November 2021) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 2w52 is ON HOLD
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==2 beta-glucans (6-O-glucosyl-laminaritriose) in both donor and acceptor sites of GH16 Laminarinase 16A from Phanerochaete chrysosporium.==
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<StructureSection load='2w52' size='340' side='right'caption='[[2w52]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2w52]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W52 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=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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;'>[[2w39|2w39]], [[2cl2|2cl2]]</div></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Endo-1,3(4)-beta-glucanase Endo-1,3(4)-beta-glucanase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.6 3.2.1.6] </span></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=2w52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w52 OCA], [https://pdbe.org/2w52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w52 RCSB], [https://www.ebi.ac.uk/pdbsum/2w52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w52 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/w5/2w52_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=2w52 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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The 1,3(4)-beta-D-glucanases of glycoside hydrolase family 16 provide useful examples of versatile yet specific protein-carbohydrate interactions. In the present study, we report the X-ray structures of the 1,3(4)-beta-D-glucanase Phanerochaete chrysosporium Laminarinase 16A in complex with beta-glucan products from laminarin (1.6 A) and lichenin (1.1 A) hydrolysis. The G6G3G3G glucan, in complex with the enzyme, showed a beta-1,6 branch in the acceptor site. The G4G3G ligand-protein complex showed that there was no room for a beta-1,6 branch in the -1 or -2 subsites; furthermore, the distorted residue in the -1 subsite and the glucose in the -2 subsite required a beta-1,3 bond between them. These are the first X-ray crystal structures of any 1,3(4)-beta-D-glucanase in complex with glucan products. They provide details of both substrate and product binding in support of earlier enzymatic evidence.
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Authors: Vasur, J., Kawai, R., Andersson, E., Igarashi, K., Sandgren, M., Samejima, M., Stahlberg, J.
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X-ray crystal structures of Phanerochaete chrysosporium Laminarinase 16A in complex with products from lichenin and laminarin hydrolysis.,Vasur J, Kawai R, Andersson E, Igarashi K, Sandgren M, Samejima M, Stahlberg J FEBS J. 2009 Jul;276(14):3858-69. Epub 2009 Jun 17. PMID:19769746<ref>PMID:19769746</ref>
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Description: 2 beta-glucans (6-O-glucosyl-laminaritriose) in both donor and acceptor sites of GH16 Laminarinase 16A from Phanerochaete chrysosporium.
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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 Dec 10 14:20:07 2008''
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<div class="pdbe-citations 2w52" 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: Large Structures]]
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[[Category: Andersson, E]]
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[[Category: Igarashi, K]]
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[[Category: Kawai, R]]
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[[Category: Samejima, M]]
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[[Category: Sandgren, M]]
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[[Category: Stahlberg, J]]
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[[Category: Vasur, J]]
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[[Category: 3/1]]
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[[Category: 6-glucan]]
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[[Category: Basidiomycete]]
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[[Category: Beta sandwich]]
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[[Category: Beta- glucanase]]
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[[Category: Beta-1\]]
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[[Category: Extracellular]]
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[[Category: Family 16]]
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[[Category: Gh16]]
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[[Category: Gh7]]
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[[Category: Glycosyl hydrolase]]
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[[Category: Hydrolase]]
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[[Category: Lam16a]]
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[[Category: Laminarin]]

Current revision

2 beta-glucans (6-O-glucosyl-laminaritriose) in both donor and acceptor sites of GH16 Laminarinase 16A from Phanerochaete chrysosporium.

PDB ID 2w52

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