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6tn6
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==X-ray structure of the endo-beta-1,4-mannanase from Thermotoga petrophila== | ==X-ray structure of the endo-beta-1,4-mannanase from Thermotoga petrophila== | ||
| - | <StructureSection load='6tn6' size='340' side='right'caption='[[6tn6]]' scene=''> | + | <StructureSection load='6tn6' size='340' side='right'caption='[[6tn6]], [[Resolution|resolution]] 1.45Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TN6 OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6tn6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_petrophila_RKU-1 Thermotoga petrophila RKU-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TN6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TN6 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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=6tn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tn6 OCA], [https://pdbe.org/6tn6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tn6 RCSB], [https://www.ebi.ac.uk/pdbsum/6tn6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tn6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A5IMX7_THEP1 A5IMX7_THEP1] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The endo-beta-1,4-mannanase from the hyperthermostable bacterium Thermotoga petrophila (TpMan) is an enzyme that catalyzes the hydrolysis of mannan and heteromannan polysaccharides. Of the three domains that comprise TpMan, the N-terminal GH5 catalytic domain and the C-terminal carbohydrate-binding domain are connected through a central ancillary domain of unknown structure and function. In this study, we report the partial crystal structure of the TpMan at 1.45 A resolution, so far, the first modular hyperthermostable endo-beta-1,4-mannanase structure determined. The structure exhibits two domains, a (beta/alpha)8-barrel GH5 catalytic domain connected via a linker to the central domain with an immunoglobulin-like beta-sandwich fold formed of seven beta-strands. Functional analysis showed that whereas the immunoglobulin-like domain does not have the carbohydrate-binding function, it stacks on the GH5 catalytic domain acting as a thermostabilizing domain and allowing operation at hyperthermophilic conditions. The carbohydrate-binding domain is absent in the crystal structure most likely due to its high flexibility around the immunoglobulin-like domain which may act also as a pivot. These results represent new structural and functional information useful on biotechnological applications for biofuel and food industries. | ||
| + | |||
| + | High-resolution structure of a modular hyperthermostable endo-beta-1,4-mannanase from Thermotoga petrophila: The ancillary immunoglobulin-like module is a thermostabilizing domain.,da Silva VM, Cabral AD, Speranca MA, Squina FM, Muniz JRC, Martin L, Nicolet Y, Garcia W Biochim Biophys Acta Proteins Proteom. 2020 Apr 21;1868(8):140437. doi:, 10.1016/j.bbapap.2020.140437. PMID:32325255<ref>PMID:32325255</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6tn6" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Thermotoga petrophila RKU-1]] | ||
[[Category: Garcia W]] | [[Category: Garcia W]] | ||
[[Category: Martin L]] | [[Category: Martin L]] | ||
Current revision
X-ray structure of the endo-beta-1,4-mannanase from Thermotoga petrophila
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