2w52
From Proteopedia
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- | [[ | + | ==2 beta-glucans (6-O-glucosyl-laminaritriose) in both donor and acceptor sites of GH16 Laminarinase 16A from Phanerochaete chrysosporium.== |
+ | <StructureSection load='2w52' size='340' side='right' caption='[[2w52]], [[Resolution|resolution]] 1.56Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[2w52]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phanerochaete_chrysosporium Phanerochaete chrysosporium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W52 OCA]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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><br> | ||
+ | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2w39|2w39]], [[2cl2|2cl2]]</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2w52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w52 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2w52 RCSB], [http://www.ebi.ac.uk/pdbsum/2w52 PDBsum]</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/w5/2w52_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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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. | ||
- | + | 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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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
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- | == | + | |
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[[Category: Phanerochaete chrysosporium]] | [[Category: Phanerochaete chrysosporium]] | ||
[[Category: Andersson, E.]] | [[Category: Andersson, E.]] |
Revision as of 08:34, 7 May 2014
2 beta-glucans (6-O-glucosyl-laminaritriose) in both donor and acceptor sites of GH16 Laminarinase 16A from Phanerochaete chrysosporium.
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Categories: Phanerochaete chrysosporium | Andersson, E. | Igarashi, K. | Kawai, R. | Samejima, M. | Sandgren, M. | Stahlberg, J. | Vasur, J. | 3/1 | 6-glucan | Basidiomycete | Beta sandwich | Beta- glucanase | Beta-1\ | Extracellular | Family 16 | Gh16 | Gh7 | Glycosyl hydrolase | Hydrolase | Lam16a | Laminarin