View source for 1xbd


==INTERNAL XYLAN BINDING DOMAIN FROM CELLULOMONAS FIMI XYLANASE D, NMR, 5 STRUCTURES==
<StructureSection load='1xbd' size='340' side='right'caption='[[1xbd]]' scene=''>
== Structural highlights ==
<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>
</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>
<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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== 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/1xbd_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1xbd ConSurf].
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cellulomonas fimi]]
[[Category: Large Structures]]
[[Category: Bolam DN]]
[[Category: Ciruela A]]
[[Category: Cooper A]]
[[Category: Gilbert HJ]]
[[Category: Hazlewood GP]]
[[Category: Simpson PJ]]
[[Category: Williamson MP]]