3amc

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<StructureSection load='3amc' size='340' side='right'caption='[[3amc]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
<StructureSection load='3amc' size='340' side='right'caption='[[3amc]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3amc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AMC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3amc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AMC FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3amd|3amd]], [[3amg|3amg]], [[3aof|3aof]], [[3azr|3azr]], [[3azs|3azs]], [[3azt|3azt]]</div></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]] 1.4&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM_1751 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [https://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=3amc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3amc OCA], [https://pdbe.org/3amc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3amc RCSB], [https://www.ebi.ac.uk/pdbsum/3amc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3amc ProSAT]</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=3amc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3amc OCA], [https://pdbe.org/3amc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3amc RCSB], [https://www.ebi.ac.uk/pdbsum/3amc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3amc ProSAT]</span></td></tr>
</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/Q9X273_THEMA Q9X273_THEMA]
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The hyperthermophilic endoglucanase Cel5A from Thermotoga maritima can find applications in lignocellulosic biofuel production, because it catalyzes the hydrolysis of glucan- and mannan-based polysaccharides. Here, we report the crystal structures in apo-form and in complex with three ligands, cellotetraose, cellobiose and mannotriose, at 1.29A to 2.40A resolution. The open carbohydrate-binding cavity which can accommodate oligosaccharide substrates with extensively branched chains explained the dual specificity of the enzyme. Combining our structural information and the previous kinetic data, it is suggested that this enzyme prefers beta-glucosyl and beta-mannosyl moieties at the reducing end and uses two conserved catalytic residues, E253 (nucleophile) and E136 (general acid/base), to hydrolyze the glycosidic bonds. Moreover, our results also suggest that the wide spectrum of Tm_Cel5A substrates might be due to the lack of steric hindrance around the C2-hydroxyl group of the glucose or mannose unit from active-site residues.
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Diverse substrate recognition mechanism revealed by Thermotoga maritima Cel5A structures in complex with cellotetraose, cellobiose and mannotriose.,Wu TH, Huang CH, Ko TP, Lai HL, Ma Y, Chen CC, Cheng YS, Liu JR, Guo RT Biochim Biophys Acta. 2011 Dec;1814(12):1832-40. doi:, 10.1016/j.bbapap.2011.07.020. Epub 2011 Aug 4. PMID:21839861<ref>PMID:21839861</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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</div>
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<div class="pdbe-citations 3amc" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Glucanase 3D structures|Glucanase 3D structures]]
*[[Glucanase 3D structures|Glucanase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cellulase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Thema]]
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[[Category: Thermotoga maritima MSB8]]
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[[Category: Cheng, Y S]]
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[[Category: Cheng YS]]
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[[Category: Guo, R T]]
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[[Category: Guo RT]]
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[[Category: Huang, C H]]
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[[Category: Huang CH]]
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[[Category: Ko, T P]]
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[[Category: Ko TP]]
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[[Category: Lai, H L]]
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[[Category: Lai HL]]
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[[Category: Liu, J R]]
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[[Category: Liu JR]]
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[[Category: Ma, Y]]
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[[Category: Ma Y]]
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[[Category: Wu, T H]]
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[[Category: Wu TH]]
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[[Category: Biofuel]]
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[[Category: Glycosyl hydrolase family 5]]
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[[Category: Hydrolase]]
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[[Category: Hyperthermostable]]
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Current revision

Crystal structures of Thermotoga maritima Cel5A, apo form and dimer/au

PDB ID 3amc

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