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| | <StructureSection load='2bo6' size='340' side='right'caption='[[2bo6]], [[Resolution|resolution]] 2.45Å' scene=''> | | <StructureSection load='2bo6' size='340' side='right'caption='[[2bo6]], [[Resolution|resolution]] 2.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2bo6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43812 Atcc 43812]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BO6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2bo6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodothermus_marinus Rhodothermus marinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BO6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DGY:(2R)-2,3-DIHYDROXYPROPANOIC+ACID'>DGY</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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]] 2.45Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2bo4|2bo4]], [[2bo7|2bo7]], [[2bo8|2bo8]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DGY:(2R)-2,3-DIHYDROXYPROPANOIC+ACID'>DGY</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=2bo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bo6 OCA], [https://pdbe.org/2bo6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bo6 RCSB], [https://www.ebi.ac.uk/pdbsum/2bo6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bo6 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=2bo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bo6 OCA], [https://pdbe.org/2bo6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bo6 RCSB], [https://www.ebi.ac.uk/pdbsum/2bo6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bo6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/MGS_RHOMR MGS_RHOMR]] Involved in the biosynthesis of the stress protectant 2-O-alpha-D-mannosyl glycerate (MG) which is produced in response to growth at supraoptimal temperature and salinity, and protects several enzymes against inactivation by temperature, freeze-drying and osmotic stress. Catalyzes the condensation of alpha-GDP-D-mannose (GDP-Man) with D-glycerate to produce alpha-mannosyl-D-glycerate. It is specific for GDP-Man, but it can also use alpha-GDP-D-glucose (GDP-Glc), beta-GDP-D-fuctose, alpha-UDP-D-mannose and alpha-UDP-D-glucose as sugar donors. It is specific for D-glycerate, but it can also use D-lactate and glycolate as sugar acceptors. This reaction occurs with a net retention of anomeric configuration; the newly formed glycosidic linkage has the same alpha configuration as the sugar donor.<ref>PMID:10585410</ref> <ref>PMID:15951819</ref> <ref>PMID:21288903</ref>
| + | [https://www.uniprot.org/uniprot/MGS_RHOMR MGS_RHOMR] Involved in the biosynthesis of the stress protectant 2-O-alpha-D-mannosyl glycerate (MG) which is produced in response to growth at supraoptimal temperature and salinity, and protects several enzymes against inactivation by temperature, freeze-drying and osmotic stress. Catalyzes the condensation of alpha-GDP-D-mannose (GDP-Man) with D-glycerate to produce alpha-mannosyl-D-glycerate. It is specific for GDP-Man, but it can also use alpha-GDP-D-glucose (GDP-Glc), beta-GDP-D-fuctose, alpha-UDP-D-mannose and alpha-UDP-D-glucose as sugar donors. It is specific for D-glycerate, but it can also use D-lactate and glycolate as sugar acceptors. This reaction occurs with a net retention of anomeric configuration; the newly formed glycosidic linkage has the same alpha configuration as the sugar donor.<ref>PMID:10585410</ref> <ref>PMID:15951819</ref> <ref>PMID:21288903</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 43812]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bolam, D N]] | + | [[Category: Rhodothermus marinus]] |
| - | [[Category: Davies, G J]] | + | [[Category: Bolam DN]] |
| - | [[Category: Davis, B G]] | + | [[Category: Davies GJ]] |
| - | [[Category: Dodson, E J]] | + | [[Category: Davis BG]] |
| - | [[Category: Flint, J]] | + | [[Category: Dodson EJ]] |
| - | [[Category: Gilbert, H J]] | + | [[Category: Flint J]] |
| - | [[Category: Martinez-Fleites, C]] | + | [[Category: Gilbert HJ]] |
| - | [[Category: Tailford, L E]] | + | [[Category: Martinez-Fleites C]] |
| - | [[Category: Taylor, E]] | + | [[Category: Tailford LE]] |
| - | [[Category: Yang, M]] | + | [[Category: Taylor E]] |
| - | [[Category: Catalysis]]
| + | [[Category: Yang M]] |
| - | [[Category: Glycosyltransferase]]
| + | |
| - | [[Category: Mannose]]
| + | |
| - | [[Category: Stereoselectivity]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
MGS_RHOMR Involved in the biosynthesis of the stress protectant 2-O-alpha-D-mannosyl glycerate (MG) which is produced in response to growth at supraoptimal temperature and salinity, and protects several enzymes against inactivation by temperature, freeze-drying and osmotic stress. Catalyzes the condensation of alpha-GDP-D-mannose (GDP-Man) with D-glycerate to produce alpha-mannosyl-D-glycerate. It is specific for GDP-Man, but it can also use alpha-GDP-D-glucose (GDP-Glc), beta-GDP-D-fuctose, alpha-UDP-D-mannose and alpha-UDP-D-glucose as sugar donors. It is specific for D-glycerate, but it can also use D-lactate and glycolate as sugar acceptors. This reaction occurs with a net retention of anomeric configuration; the newly formed glycosidic linkage has the same alpha configuration as the sugar donor.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The enzymatic transfer of activated mannose yields mannosides in glycoconjugates and oligo- and polysaccharides. Yet, despite its biological necessity, the mechanism by which glycosyltransferases recognize mannose and catalyze its transfer to acceptor molecules is poorly understood. Here, we report broad high-throughput screening and kinetic analyses of both natural and synthetic substrates of Rhodothermus marinus mannosylglycerate synthase (MGS), which catalyzes the formation of the stress protectant 2-O-alpha-D-mannosyl glycerate. The sequence of MGS indicates that it is at the cusp of inverting and retaining transferases. The structures of apo MGS and complexes with donor and acceptor molecules, including GDP-mannose, combined with mutagenesis of the binding and catalytic sites, unveil the mannosyl transfer center. Nucleotide specificity is as important in GDP-D-mannose recognition as the nature of the donor sugar.
Structural dissection and high-throughput screening of mannosylglycerate synthase.,Flint J, Taylor E, Yang M, Bolam DN, Tailford LE, Martinez-Fleites C, Dodson EJ, Davis BG, Gilbert HJ, Davies GJ Nat Struct Mol Biol. 2005 Jul;12(7):608-14. Epub 2005 Jun 12. PMID:15951819[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Martins LO, Empadinhas N, Marugg JD, Miguel C, Ferreira C, da Costa MS, Santos H. Biosynthesis of mannosylglycerate in the thermophilic bacterium Rhodothermus marinus. Biochemical and genetic characterization of a mannosylglycerate synthase. J Biol Chem. 1999 Dec 10;274(50):35407-14. PMID:10585410
- ↑ Flint J, Taylor E, Yang M, Bolam DN, Tailford LE, Martinez-Fleites C, Dodson EJ, Davis BG, Gilbert HJ, Davies GJ. Structural dissection and high-throughput screening of mannosylglycerate synthase. Nat Struct Mol Biol. 2005 Jul;12(7):608-14. Epub 2005 Jun 12. PMID:15951819 doi:http://dx.doi.org/10.1038/nsmb950
- ↑ Nielsen MM, Suits MD, Yang M, Barry CS, Martinez-Fleites C, Tailford LE, Flint JE, Dumon C, Davis BG, Gilbert HJ, Davies GJ. Substrate and metal ion promiscuity in mannosylglycerate synthase. J Biol Chem. 2011 Apr 29;286(17):15155-64. Epub 2011 Feb 2. PMID:21288903 doi:10.1074/jbc.M110.199844
- ↑ Flint J, Taylor E, Yang M, Bolam DN, Tailford LE, Martinez-Fleites C, Dodson EJ, Davis BG, Gilbert HJ, Davies GJ. Structural dissection and high-throughput screening of mannosylglycerate synthase. Nat Struct Mol Biol. 2005 Jul;12(7):608-14. Epub 2005 Jun 12. PMID:15951819 doi:http://dx.doi.org/10.1038/nsmb950
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