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| | ==Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum.== | | ==Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum.== |
| - | <StructureSection load='5n6u' size='340' side='right' caption='[[5n6u]], [[Resolution|resolution]] 3.08Å' scene=''> | + | <StructureSection load='5n6u' size='340' side='right'caption='[[5n6u]], [[Resolution|resolution]] 3.08Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5n6u]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Dict6 Dict6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N6U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N6U FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5n6u]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyoglomus_thermophilum_H-6-12 Dictyoglomus thermophilum H-6-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N6U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N6U FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.08Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DICTH_1692 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=309799 DICT6])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-mannosidase Beta-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.25 3.2.1.25] </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=5n6u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n6u OCA], [https://pdbe.org/5n6u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n6u RCSB], [https://www.ebi.ac.uk/pdbsum/5n6u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n6u ProSAT]</span></td></tr> |
| - | <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=5n6u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n6u OCA], [http://pdbe.org/5n6u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n6u RCSB], [http://www.ebi.ac.uk/pdbsum/5n6u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n6u ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B5YAN4_DICT6 B5YAN4_DICT6] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Mannosidase|Mannosidase]] | + | *[[Mannosidase 3D structures|Mannosidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Beta-mannosidase]] | + | [[Category: Dictyoglomus thermophilum H-6-12]] |
| - | [[Category: Dict6]] | + | [[Category: Large Structures]] |
| - | [[Category: Lafite, P]] | + | [[Category: Lafite P]] |
| - | [[Category: Richet, N]] | + | [[Category: Richet N]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Mannosidase]]
| + | |
| - | [[Category: Thermostable]]
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| Structural highlights
Function
B5YAN4_DICT6
Publication Abstract from PubMed
Glycoside hydrolases can be turned into thioglycoligase by mutation of the acid/base catalytic carboxylate residue. These mutants have proven valuable to generate S-glycosides, however, few examples in literature have described efficient thioglycoligase activity, and even fewer the underlying molecular mechanism. DtMan, a GH2 family beta-D-mannosidase from the thermophilic Dictyoglomus thermophilum was cloned and expressed in E. coli. The recombinant protein is highly specific for beta-D-mannosides, and exhibits efficient catalysis constants coupled to thermostability. However, seven variants bearing mutated acid/base residue could not be turned into efficient thioligases. Crystal structure of DtMan Glu425Cys mutant and molecular modeling calculations have demonstrated that unlike other GH2 thioligase reported, active site accessibility of thiol acceptor may be impaired by entrance loop rigidity. This structural feature may explain why DtMan mutants do not exhibit thioglycoligase activity.
Is the acid/base catalytic residue mutation in beta-D-mannosidase DtMan from Dictyoglomus thermophilum sufficient enough to provide thioglycoligase activity?,Guillotin L, Richet N, Lafite P, Daniellou R Biochimie. 2017 Apr 3. pii: S0300-9084(17)30085-8. doi:, 10.1016/j.biochi.2017.03.020. PMID:28385558[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Guillotin L, Richet N, Lafite P, Daniellou R. Is the acid/base catalytic residue mutation in beta-D-mannosidase DtMan from Dictyoglomus thermophilum sufficient enough to provide thioglycoligase activity? Biochimie. 2017 Apr 3. pii: S0300-9084(17)30085-8. doi:, 10.1016/j.biochi.2017.03.020. PMID:28385558 doi:http://dx.doi.org/10.1016/j.biochi.2017.03.020
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