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New page: left|200px<br /><applet load="1qld" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qld" /> '''SOLUTION STRUCTURE OF TYPE X CBM'''<br /> =...
 
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[[Image:1qld.jpg|left|200px]]<br /><applet load="1qld" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1qld" />
'''SOLUTION STRUCTURE OF TYPE X CBM'''<br />


==Overview==
==Solution structure of type X CBM==
Plant cell wall hydrolases generally have a modular structure consisting, of a catalytic domain linked to one or more noncatalytic, carbohydrate-binding modules (CBMs), whose common function is to attach, the enzyme to the polymeric substrate. Xylanase A from Pseudomonas, fluorescens subsp. cellulosa (Pf Xyn10A) consists of a family 10 catalytic, domain, an N-terminal family IIa cellulose-binding module, and an internal, family 10 cellulose-binding module. The structure of the 45-residue family, 10 CBM has been determined in solution using NMR. It consists of two, antiparallel beta-sheets, one with two strands and one with three, with a, short alpha-helix across one face of the three-stranded sheet. There is a, high density of aromatic residues on one side of the protein, including, three aromatic residues (Tyr8, Trp22, and Trp24), which are exposed and, form a flat surface on one face, in a classical polysaccharide-binding, arrangement. The fold is closely similar to that of the, oligonucleotide/oligosaccharide-binding (OB) fold, but appears to have, arisen by convergent evolution, because there is no sequence similarity, and the presumed binding sites are on different faces.
<StructureSection load='1qld' size='340' side='right'caption='[[1qld]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1qld]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QLD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QLD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</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=1qld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qld OCA], [https://pdbe.org/1qld PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qld RCSB], [https://www.ebi.ac.uk/pdbsum/1qld PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qld ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/XYNA_CELJU XYNA_CELJU]
== 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/ql/1qld_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=1qld ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Plant cell wall hydrolases generally have a modular structure consisting of a catalytic domain linked to one or more noncatalytic carbohydrate-binding modules (CBMs), whose common function is to attach the enzyme to the polymeric substrate. Xylanase A from Pseudomonas fluorescens subsp. cellulosa (Pf Xyn10A) consists of a family 10 catalytic domain, an N-terminal family IIa cellulose-binding module, and an internal family 10 cellulose-binding module. The structure of the 45-residue family 10 CBM has been determined in solution using NMR. It consists of two antiparallel beta-sheets, one with two strands and one with three, with a short alpha-helix across one face of the three-stranded sheet. There is a high density of aromatic residues on one side of the protein, including three aromatic residues (Tyr8, Trp22, and Trp24), which are exposed and form a flat surface on one face, in a classical polysaccharide-binding arrangement. The fold is closely similar to that of the oligonucleotide/oligosaccharide-binding (OB) fold, but appears to have arisen by convergent evolution, because there is no sequence similarity, and the presumed binding sites are on different faces.


==About this Structure==
Solution structure of the CBM10 cellulose binding module from Pseudomonas xylanase A.,Raghothama S, Simpson PJ, Szabo L, Nagy T, Gilbert HJ, Williamson MP Biochemistry. 2000 Feb 8;39(5):978-84. PMID:10653641<ref>PMID:10653641</ref>
1QLD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. 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=1QLD OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Solution structure of the CBM10 cellulose binding module from Pseudomonas xylanase A., Raghothama S, Simpson PJ, Szabo L, Nagy T, Gilbert HJ, Williamson MP, Biochemistry. 2000 Feb 8;39(5):978-84. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10653641 10653641]
</div>
[[Category: Endo-1,4-beta-xylanase]]
<div class="pdbe-citations 1qld" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas fluorescens]]
[[Category: Pseudomonas fluorescens]]
[[Category: Single protein]]
[[Category: Gilbert HJ]]
[[Category: Gilbert, H.J.]]
[[Category: Raghothama S]]
[[Category: Raghothama, S.]]
[[Category: Simpson PJ]]
[[Category: Simpson, P.J.]]
[[Category: Williamson MP]]
[[Category: Williamson, M.P.]]
[[Category: anti parallel beta sheets]]
[[Category: beta strands]]
[[Category: glycosidase]]
[[Category: hydrolase]]
[[Category: xylan degradation]]
 
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