1xbd

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(New page: 200px<br /><applet load="1xbd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xbd" /> '''INTERNAL XYLAN BINDING DOMAIN FROM CELLULOMO...)
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[[Image:1xbd.jpg|left|200px]]<br /><applet load="1xbd" size="450" color="white" frame="true" align="right" spinBox="true"
 
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'''INTERNAL XYLAN BINDING DOMAIN FROM CELLULOMONAS FIMI XYLANASE D, NMR, 5 STRUCTURES'''<br />
 
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==Overview==
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==INTERNAL XYLAN BINDING DOMAIN FROM CELLULOMONAS FIMI XYLANASE D, NMR, 5 STRUCTURES==
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BACKGROUND: Many enzymes that digest polysaccharides contain separate, polysaccharide-binding domains. Structures have been previously determined, for a number of cellulose-binding domains (CBDs) from cellulases. RESULTS:, The family IIb xylan-binding domain 1 (XBD1) from Cellulomonas fimi, xylanase D is shown to bind xylan but not cellulose. Its structure is, similar to that of the homologous family IIa CBD from C. fimi Cex, consisting of two four-stranded beta sheets that form a twisted 'beta, sandwich'. The xylan-binding site is a groove made from two tryptophan, residues that stack against the faces of the sugar rings, plus several, hydrogen-bonding polar residues. CONCLUSIONS: The biggest difference, between the family IIa and IIb domains is that in the former the, solvent-exposed tryptophan sidechains are coplanar, whereas in the latter, they are perpendicular, forming a twisted binding site. The binding sites, are therefore complementary to the secondary structures of the ligands, cellulose and xylan. XBD1 and CexCBD represent a striking example of two, proteins that have high sequence similarity but a different function.
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<StructureSection load='1xbd' size='340' side='right'caption='[[1xbd]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1xbd]] 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=1XBD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XBD FirstGlance]. <br>
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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, 5 models</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=1xbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xbd OCA], [https://pdbe.org/1xbd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xbd RCSB], [https://www.ebi.ac.uk/pdbsum/1xbd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xbd ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/XYND_CELFI XYND_CELFI] Endo-acting xylanase which displays no detectable activity against polysaccharides other than xylan. Hydrolyzes glucosidic bonds with retention of anomeric configuration.
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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/xb/1xbd_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1xbd 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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BACKGROUND: Many enzymes that digest polysaccharides contain separate polysaccharide-binding domains. Structures have been previously determined for a number of cellulose-binding domains (CBDs) from cellulases. RESULTS: The family IIb xylan-binding domain 1 (XBD1) from Cellulomonas fimi xylanase D is shown to bind xylan but not cellulose. Its structure is similar to that of the homologous family IIa CBD from C. fimi Cex, consisting of two four-stranded beta sheets that form a twisted 'beta sandwich'. The xylan-binding site is a groove made from two tryptophan residues that stack against the faces of the sugar rings, plus several hydrogen-bonding polar residues. CONCLUSIONS: The biggest difference between the family IIa and IIb domains is that in the former the solvent-exposed tryptophan sidechains are coplanar, whereas in the latter they are perpendicular, forming a twisted binding site. The binding sites are therefore complementary to the secondary structures of the ligands cellulose and xylan. XBD1 and CexCBD represent a striking example of two proteins that have high sequence similarity but a different function.
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==About this Structure==
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A family IIb xylan-binding domain has a similar secondary structure to a homologous family IIa cellulose-binding domain but different ligand specificity.,Simpson PJ, Bolam DN, Cooper A, Ciruela A, Hazlewood GP, Gilbert HJ, Williamson MP Structure. 1999 Jul 15;7(7):853-64. PMID:10425686<ref>PMID:10425686</ref>
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1XBD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cellulomonas_fimi Cellulomonas fimi]. Active as [http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XBD OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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A family IIb xylan-binding domain has a similar secondary structure to a homologous family IIa cellulose-binding domain but different ligand specificity., Simpson PJ, Bolam DN, Cooper A, Ciruela A, Hazlewood GP, Gilbert HJ, Williamson MP, Structure. 1999 Jul 15;7(7):853-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10425686 10425686]
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</div>
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<div class="pdbe-citations 1xbd" 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>
[[Category: Cellulomonas fimi]]
[[Category: Cellulomonas fimi]]
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[[Category: Endo-1,4-beta-xylanase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Bolam DN]]
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[[Category: Bolam, D.N.]]
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[[Category: Ciruela A]]
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[[Category: Ciruela, A.]]
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[[Category: Cooper A]]
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[[Category: Cooper, A.]]
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[[Category: Gilbert HJ]]
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[[Category: Gilbert, H.J.]]
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[[Category: Hazlewood GP]]
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[[Category: Hazlewood, G.P.]]
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[[Category: Simpson PJ]]
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[[Category: Simpson, P.J.]]
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[[Category: Williamson MP]]
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[[Category: Williamson, M.P.]]
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[[Category: beta-sheet]]
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[[Category: hydrolase]]
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[[Category: xylan binding domain]]
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[[Category: xylanase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:57:49 2007''
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Current revision

INTERNAL XYLAN BINDING DOMAIN FROM CELLULOMONAS FIMI XYLANASE D, NMR, 5 STRUCTURES

PDB ID 1xbd

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