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2xbd
From Proteopedia
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| - | [[Image:2xbd.gif|left|200px]]<br /> | ||
| - | <applet load="2xbd" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2xbd" /> | ||
| - | '''INTERNAL XYLAN BINDING DOMAIN FROM CELLULOMONAS FIMI XYLANASE D, NMR, MINIMIZED AVERAGE STRUCTURE'''<br /> | ||
| - | == | + | ==INTERNAL XYLAN BINDING DOMAIN FROM CELLULOMONAS FIMI XYLANASE D, NMR, MINIMIZED AVERAGE STRUCTURE== |
| - | BACKGROUND: Many enzymes that digest polysaccharides contain separate | + | <StructureSection load='2xbd' size='340' side='right'caption='[[2xbd]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2xbd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_fimi"_mcbeth_and_scales_1913 "bacterium fimi" mcbeth and scales 1913]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XBD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XBD FirstGlance]. <br> | ||
| + | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xbd OCA], [https://pdbe.org/2xbd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xbd RCSB], [https://www.ebi.ac.uk/pdbsum/2xbd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xbd ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[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. | ||
| + | == 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/xb/2xbd_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/main_output.php?pdb_ID=2xbd ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 2xbd" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bacterium fimi mcbeth and scales 1913]] | ||
[[Category: Endo-1,4-beta-xylanase]] | [[Category: Endo-1,4-beta-xylanase]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Bolam, D | + | [[Category: Bolam, D N]] |
| - | [[Category: Ciruela, A | + | [[Category: Ciruela, A]] |
| - | [[Category: Cooper, A | + | [[Category: Cooper, A]] |
| - | [[Category: Gilbert, H | + | [[Category: Gilbert, H J]] |
| - | [[Category: Hazlewood, G | + | [[Category: Hazlewood, G P]] |
| - | [[Category: Simpson, P | + | [[Category: Simpson, P J]] |
| - | [[Category: Williamson, M | + | [[Category: Williamson, M P]] |
| - | [[Category: | + | [[Category: Beta-sheet]] |
| - | [[Category: | + | [[Category: Hydrolase]] |
| - | [[Category: | + | [[Category: Xylan binding domain]] |
| - | [[Category: | + | [[Category: Xylanase]] |
| - | + | ||
| - | + | ||
Current revision
INTERNAL XYLAN BINDING DOMAIN FROM CELLULOMONAS FIMI XYLANASE D, NMR, MINIMIZED AVERAGE STRUCTURE
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