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1exp

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(New page: 200px<br /> <applet load="1exp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1exp, resolution 1.8&Aring;" /> '''BETA-1,4-GLYCANASE C...)
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[[Image:1exp.gif|left|200px]]<br />
 
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<applet load="1exp" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1exp, resolution 1.8&Aring;" />
 
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'''BETA-1,4-GLYCANASE CEX-CD'''<br />
 
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==Overview==
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==BETA-1,4-GLYCANASE CEX-CD==
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The three-dimensional structure of a catalytically competent, glycosyl-enzyme intermediate of a retaining beta-1,4-glycanase has been, determined at a resolution of 1.8 A by X-ray diffraction. A fluorinated, slow substrate forms an alpha-D-glycopyranosyl linkage to one of the two, invariant carboxylates, Glu 233, as supported in solution by 19F-NMR, studies. The resulting ester linkage is coplanar with the cyclic oxygen of, the proximal saccharide and is inferred to form a strong hydrogen bond, with the 2-hydroxyl of that saccharide unit in natural substrates. The, active-site architecture of this covalent intermediate gives insights into, both the classical double-displacement catalytic mechanism and the basis, for the enzyme's specificity.
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<StructureSection load='1exp' size='340' side='right'caption='[[1exp]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1exp]] 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=1EXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EXP FirstGlance]. <br>
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1EXP is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Cellulomonas_fimi Cellulomonas fimi]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EXP OCA]].
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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]] 1.8&#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=G2F:2-DEOXY-2-FLUORO-ALPHA-D-GLUCOPYRANOSE'>G2F</scene>, <scene name='pdbligand=PRD_900050:2-deoxy-2-fluoro-beta-cellobiose'>PRD_900050</scene></td></tr>
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==Reference==
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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=1exp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1exp OCA], [https://pdbe.org/1exp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1exp RCSB], [https://www.ebi.ac.uk/pdbsum/1exp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1exp ProSAT]</span></td></tr>
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Crystallographic observation of a covalent catalytic intermediate in a beta-glycosidase., White A, Tull D, Johns K, Withers SG, Rose DR, Nat Struct Biol. 1996 Feb;3(2):149-54. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8564541 8564541]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GUX_CELFI GUX_CELFI] Hydrolyzes both cellulose and xylan. Has also weak endoglucanase activity. 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/ex/1exp_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=1exp ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Cellulomonas fimi]]
[[Category: Cellulomonas fimi]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Johns, K.L.]]
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[[Category: Johns KL]]
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[[Category: Rose, D.R.]]
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[[Category: Rose DR]]
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[[Category: Tull, D.]]
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[[Category: Tull D]]
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[[Category: White, A.]]
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[[Category: White A]]
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[[Category: Withers, S.G.]]
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[[Category: Withers SG]]
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[[Category: cellulose degradation]]
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[[Category: glycosidase]]
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[[Category: hydrolase]]
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[[Category: repeat]]
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[[Category: signal]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 19:45:41 2007''
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Current revision

BETA-1,4-GLYCANASE CEX-CD

PDB ID 1exp

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