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| | <StructureSection load='3f1y' size='340' side='right'caption='[[3f1y]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='3f1y' size='340' side='right'caption='[[3f1y]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3f1y]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F1Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F1Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3f1y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rubrobacter_xylanophilus Rubrobacter xylanophilus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F1Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F1Y FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3e25|3e25]], [[3e26|3e26]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Mannosyl-3-phosphoglycerate_synthase Mannosyl-3-phosphoglycerate synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.217 2.4.1.217] </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=3f1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f1y OCA], [https://pdbe.org/3f1y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f1y RCSB], [https://www.ebi.ac.uk/pdbsum/3f1y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f1y 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=3f1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f1y OCA], [https://pdbe.org/3f1y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f1y RCSB], [https://www.ebi.ac.uk/pdbsum/3f1y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f1y ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B7SY86_9ACTN B7SY86_9ACTN] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mannosyl-3-phosphoglycerate synthase]] | |
| - | [[Category: Costa, M S.da]] | |
| - | [[Category: Empadinhas, N]] | |
| - | [[Category: Macedo-Ribeiro, S]] | |
| - | [[Category: Pereira, P J.B]] | |
| - | [[Category: Gdp-mannose]] | |
| - | [[Category: Gt-81]] | |
| - | [[Category: Gt-a type glycosyltransferase]] | |
| | [[Category: Rubrobacter xylanophilus]] | | [[Category: Rubrobacter xylanophilus]] |
| - | [[Category: Transferase]] | + | [[Category: Synthetic construct]] |
| | + | [[Category: Empadinhas N]] |
| | + | [[Category: Macedo-Ribeiro S]] |
| | + | [[Category: Pereira PJB]] |
| | + | [[Category: Da Costa MS]] |
| Structural highlights
Function
B7SY86_9ACTN
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
Rubrobacter xylanophilus is the only actinobacterium known to accumulate the organic solute mannosylglycerate (MG); moreover, the accumulation of MG is constitutive. The key enzyme for MG synthesis, catalysing the conversion of GDP-mannose (GDP-Man) and D-3-phosphoglycerate (3-PGA) into the phosphorylated intermediate mannosyl-3-phosphoglycerate and GDP, was purified from R. xylanophilus cell extracts and the corresponding gene was expressed in E. coli. Despite the related solute glucosylglycerate (GG) having never been detected in R. xylanophilus, the cell extracts and the pure recombinant mannosyl-3-phosphoglycerate synthase (MpgS) could also synthesize glucosyl-3-phosphoglycerate (GPG), the precursor of GG, in agreement with the higher homology of the novel MpgS towards GPG-synthesizing mycobacterial glucosyl-3-phosphoglycerate synthases (GpgS) than towards MpgSs from hyper/thermophiles, known to accumulate MG under salt or thermal stress. To understand the specificity and substrate ambiguity of this novel enzyme, we determined the crystal structure of the unliganded MpgS and of its complexes with the nucleotide and sugar donors, at 2.2, 2.8 and 2.5 A resolution respectively. The first three-dimensional structures of a protein from this extremely gamma-radiation-resistant thermophile here reported show that MpgS (GT81 family) contains a GT-A like fold and clearly explain its nucleotide and sugar-donor specificity. In the GDP-Man complex, a flexible loop ((254) RQNRHQ(259) ), located close to the active site moves towards the incoming sugar moiety, providing the ligands for both magnesium ion co-ordination and sugar binding. A triple mutant of R. xylanophilus MpgS, mimicking the (206) PLAGE(210) loop stabilizing hydrogen bond network observed for mycobacterial GpgSs, reduces significantly the affinity to GDP-Man, implicating this loop in the sugar-donor discrimination.
Functional and structural characterization of a novel mannosyl-3-phosphoglycerate synthase from Rubrobacter xylanophilus reveals its dual substrate specificity.,Empadinhas N, Pereira PJ, Albuquerque L, Costa J, Sa-Moura B, Marques AT, Macedo-Ribeiro S, da Costa MS Mol Microbiol. 2011 Jan;79(1):76-93. doi:, 10.1111/j.1365-2958.2010.07432.x. Epub 2010 Nov 2. PMID:21166895[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Empadinhas N, Pereira PJ, Albuquerque L, Costa J, Sa-Moura B, Marques AT, Macedo-Ribeiro S, da Costa MS. Functional and structural characterization of a novel mannosyl-3-phosphoglycerate synthase from Rubrobacter xylanophilus reveals its dual substrate specificity. Mol Microbiol. 2011 Jan;79(1):76-93. doi:, 10.1111/j.1365-2958.2010.07432.x. Epub 2010 Nov 2. PMID:21166895 doi:10.1111/j.1365-2958.2010.07432.x
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