4m24

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==Crystal structure of the endo-1,4-glucanase, RBcel1, in complex with cellobiose==
==Crystal structure of the endo-1,4-glucanase, RBcel1, in complex with cellobiose==
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<StructureSection load='4m24' size='340' side='right' caption='[[4m24]], [[Resolution|resolution]] 1.39&Aring;' scene=''>
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<StructureSection load='4m24' size='340' side='right'caption='[[4m24]], [[Resolution|resolution]] 1.39&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4m24]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M24 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M24 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4m24]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultured_bacterium Uncultured bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M24 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M24 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CBI:CELLOBIOSE'>CBI</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.386&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ee9|4ee9]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=PRD_900005:beta-cellobiose'>PRD_900005</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span></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=4m24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m24 OCA], [https://pdbe.org/4m24 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m24 RCSB], [https://www.ebi.ac.uk/pdbsum/4m24 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m24 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4m24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m24 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m24 RCSB], [http://www.ebi.ac.uk/pdbsum/4m24 PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/C1JI15_9BACT C1JI15_9BACT]
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In this study, the mining of an Antarctic soil sample by functional metagenomics allowed the isolation of a cold-adapted protein (RBcel1) that hydrolyzes only carboxymethyl cellulose. The new enzyme is related to family 5 of the glycosyl hydrolase (GH5) protein from Pseudomonas stutzeri (Pst_2494) and does not possess a carbohydrate-binding domain. The protein was produced and purified to homogeneity. RBcel1 displayed an endoglucanase activity, producing cellobiose and cellotriose, using carboxymethyl cellulose as a substrate. Moreover, the study of pH and the thermal dependence of the hydrolytic activity shows that RBcel1 was active from pH 6 to pH 9 and remained significantly active when temperature decreased (18% of activity at 10 degrees C). It is interesting that RBcel1 was able to synthetize non-reticulated cellulose using cellobiose as a substrate. Moreover, by a combination of bioinformatics and enzyme analysis, the physiological relevance of the RBcel1 protein and its mesophilic homologous Pst_2494 protein from P. stutzeri, A1501, was established as the key enzymes involved in the production of cellulose by bacteria. In addition, RBcel1 and Pst_2494 are the two primary enzymes belonging to the GH5 family involved in this process.
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Insights into bacterial cellulose biosynthesis by functional metagenomics on Antarctic soil samples.,Berlemont R, Delsaute M, Pipers D, D'Amico S, Feller G, Galleni M, Power P ISME J. 2009 Sep;3(9):1070-81. doi: 10.1038/ismej.2009.48. Epub 2009 May 21. PMID:19458657<ref>PMID:19458657</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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</div>
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*[[Glucanase 3D structures|Glucanase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cellulase]]
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[[Category: Large Structures]]
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[[Category: Bauvois, C]]
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[[Category: Uncultured bacterium]]
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[[Category: Berlemont, R]]
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[[Category: Bauvois C]]
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[[Category: Delsaute, M]]
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[[Category: Berlemont R]]
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[[Category: Galleni, M]]
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[[Category: Delsaute M]]
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[[Category: Elder, D Van]]
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[[Category: Galleni M]]
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[[Category: 4-endoglucanase]]
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[[Category: Van elder D]]
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[[Category: Beta-1]]
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[[Category: Glycosyl hydrolase family 5]]
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[[Category: Hydrolase]]
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[[Category: Tim barrel]]
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Current revision

Crystal structure of the endo-1,4-glucanase, RBcel1, in complex with cellobiose

PDB ID 4m24

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