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1exh

From Proteopedia

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[[Image:1exh.gif|left|200px]]
 
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==SOLUTION STRUCTURE OF A CELLULOSE BINDING DOMAIN FROM CELLULOMONAS FIMI BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY==
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The line below this paragraph, containing "STRUCTURE_1exh", creates the "Structure Box" on the page.
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<StructureSection load='1exh' size='340' side='right'caption='[[1exh]]' 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'>[[1exh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellulomonas_fimi Cellulomonas fimi]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EXH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EXH 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">Solution NMR</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=1exh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1exh OCA], [https://pdbe.org/1exh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1exh RCSB], [https://www.ebi.ac.uk/pdbsum/1exh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1exh ProSAT]</span></td></tr>
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{{STRUCTURE_1exh| PDB=1exh | SCENE= }}
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</table>
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== Function ==
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'''SOLUTION STRUCTURE OF A CELLULOSE BINDING DOMAIN FROM CELLULOMONAS FIMI BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY'''
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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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==Overview==
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Check<jmol>
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Multidimensional, multinuclear nuclear magnetic resonance spectroscopy combined with dynamical simulated annealing has been used to determine the structure of a 110 amino acid cellulose-binding domain (CBD) from Cex, a beta-1,4-glycanase from the bacterium Cellulomonas fimi (CBDcex). An experimental data set comprising 1795 interproton NOE-derived restraints, 50 phi, 34 chi 1, and 106 hydrogen bond restraints was used to calculate 20 final structures. The calculated structures have an average root-mean-square (rms) deviation about the mean structure of 0.41 A for backbone atoms and 0.67 A for all heavy atoms when fitted over the secondary structural elements. Chromatography, ultracentrifugation, and 15N NMR relaxation experiments demonstrate that CBDcex is a dimer in solution. While attempts to measure NOEs across the dimer interface were unsuccessful, a computational strategy was employed to generate dimer structures consistent with the derived data set. The results from the dimer calculations indicate that, while the monomer topologies produced in the context of the dimer can be variable, the relative positioning of secondary structural elements and side chains present in the monomer are restored upon dimer formation. CBDcex forms an extensive beta-sheet structure with a beta-barrel fold. Titration with cellohexaose, [beta-D-glucopyranosyl-(1,4)]5-D-glucose, establishes that Trp 54 and 72 participate in cellulose binding. Analysis of the structure shows that these residues are adjacent in space and exposed to solvent. Together with other proximate hydrophilic residues, these residues form a carbohydrate-binding cleft, which appears to be a feature common to all CBDs of the same family.
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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/1exh_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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1EXH is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EXH OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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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=1exh ConSurf].
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Solution structure of a cellulose-binding domain from Cellulomonas fimi by nuclear magnetic resonance spectroscopy., Xu GY, Ong E, Gilkes NR, Kilburn DG, Muhandiram DR, Harris-Brandts M, Carver JP, Kay LE, Harvey TS, Biochemistry. 1995 May 30;34(21):6993-7009. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7766609 7766609]
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<div style="clear:both"></div>
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[[Category: Cellulose 1,4-beta-cellobiosidase]]
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__TOC__
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[[Category: Single protein]]
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</StructureSection>
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[[Category: Carver, J P.]]
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[[Category: Cellulomonas fimi]]
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[[Category: Gilkes, N R.]]
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[[Category: Large Structures]]
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[[Category: Harris-Brandts, M.]]
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[[Category: Carver JP]]
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[[Category: Harvey, T S.]]
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[[Category: Gilkes NR]]
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[[Category: Kay, L E.]]
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[[Category: Harris-Brandts M]]
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[[Category: Kilburn, D G.]]
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[[Category: Harvey TS]]
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[[Category: Muhandiram, D R.]]
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[[Category: Kay LE]]
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[[Category: Ong, E.]]
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[[Category: Kilburn DG]]
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[[Category: Xu, G Y.]]
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[[Category: Muhandiram DR]]
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[[Category: Cellulose binding domain]]
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[[Category: Ong E]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:38:13 2008''
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[[Category: Xu G-Y]]

Current revision

SOLUTION STRUCTURE OF A CELLULOSE BINDING DOMAIN FROM CELLULOMONAS FIMI BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY

PDB ID 1exh

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