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| ==Solution structure of type X CBM== | | ==Solution structure of type X CBM== |
| <StructureSection load='1qld' size='340' side='right'caption='[[1qld]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | | <StructureSection load='1qld' size='340' side='right'caption='[[1qld]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[1qld]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_liquefaciens"_flugge_1886 "bacillus fluorescens liquefaciens" flugge 1886]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1QLD FirstGlance]. <br> | | <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ct7|1ct7]], [[1clx|1clx]], [[1xys|1xys]]</td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </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=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> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1qld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qld OCA], [http://pdbe.org/1qld PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qld RCSB], [http://www.ebi.ac.uk/pdbsum/1qld PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qld ProSAT]</span></td></tr> | |
| </table> | | </table> |
| | == Function == |
| | [https://www.uniprot.org/uniprot/XYNA_CELJU XYNA_CELJU] |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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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=1qld ConSurf]. | | </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="clear:both"></div> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| 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.
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| 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>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 1qld" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Bacillus fluorescens liquefaciens flugge 1886]]
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| [[Category: Endo-1,4-beta-xylanase]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Gilbert, H J]] | | [[Category: Pseudomonas fluorescens]] |
| [[Category: Raghothama, S]] | | [[Category: Gilbert HJ]] |
| [[Category: Simpson, P J]] | | [[Category: Raghothama S]] |
| [[Category: Williamson, M P]] | | [[Category: Simpson PJ]] |
| [[Category: Anti parallel beta sheet]] | | [[Category: Williamson MP]] |
| [[Category: Beta strand]]
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| [[Category: Glycosidase]]
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| [[Category: Hydrolase]]
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| [[Category: Xylan degradation]]
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| [[Category: Xylanase]]
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