1gu3

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{{Seed}}
 
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[[Image:1gu3.png|left|200px]]
 
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==CBM4 structure and function==
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The line below this paragraph, containing "STRUCTURE_1gu3", creates the "Structure Box" on the page.
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<StructureSection load='1gu3' size='340' side='right'caption='[[1gu3]], [[Resolution|resolution]] 2.30&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'>[[1gu3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellulomonas_fimi Cellulomonas fimi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GU3 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<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=PRD_900016:beta-cellopentaose'>PRD_900016</scene></td></tr>
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{{STRUCTURE_1gu3| PDB=1gu3 | 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=1gu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gu3 OCA], [https://pdbe.org/1gu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gu3 RCSB], [https://www.ebi.ac.uk/pdbsum/1gu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gu3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GUNC_CELFA GUNC_CELFA] The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
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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/gu/1gu3_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=1gu3 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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Enzymes active on complex carbohydrate polymers frequently have modular structures in which a catalytic domain is appended to one or more carbohydrate-binding modules (CBMs). Although CBMs have been classified into a number of families based upon sequence, many closely related CBMs are specific for different polysaccharides. In order to provide a structural rationale for the recognition of different polysaccharides by CBMs displaying a conserved fold, we have studied the thermodynamics of binding and three-dimensional structures of the related family 4 CBMs from Cellulomonas fimi Cel9B and Thermotoga maritima Lam16A in complex with their ligands, beta-1,4 and beta-1,3 linked gluco-oligosaccharides, respectively. These two CBMs use a structurally conserved constellation of aromatic and polar amino acid side-chains that interact with sugars in two of the five binding subsites. Differences in the length and conformation of loops in non-conserved regions create binding-site topographies that complement the known solution conformations of their respective ligands. Thermodynamics interpreted in the light of structural information highlights the differential role of water in the interaction of these CBMs with their respective oligosaccharide ligands.
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===CBM4 STRUCTURE AND FUNCTION===
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Differential oligosaccharide recognition by evolutionarily-related beta-1,4 and beta-1,3 glucan-binding modules.,Boraston AB, Nurizzo D, Notenboom V, Ducros V, Rose DR, Kilburn DG, Davies GJ J Mol Biol. 2002 Jun 21;319(5):1143-56. PMID:12079353<ref>PMID:12079353</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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<div class="pdbe-citations 1gu3" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12079353}}, adds the Publication Abstract to the page
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*[[Glucanase 3D structures|Glucanase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12079353 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12079353}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1GU3 is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cellulomonas_fimi Cellulomonas fimi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GU3 OCA].
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==Reference==
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<ref group="xtra">PMID:12079353</ref><references group="xtra"/>
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[[Category: Cellulase]]
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[[Category: Cellulomonas fimi]]
[[Category: Cellulomonas fimi]]
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[[Category: Davies, G J.]]
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[[Category: Large Structures]]
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[[Category: Notenboom, V.]]
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[[Category: Davies GJ]]
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[[Category: Nurizzo, D.]]
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[[Category: Notenboom V]]
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[[Category: Carbohydrate binding module]]
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[[Category: Nurizzo D]]
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[[Category: Cbm]]
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[[Category: Cellulose]]
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[[Category: Glucan]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 22 14:50:57 2010''
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Current revision

CBM4 structure and function

PDB ID 1gu3

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