2bo4

From Proteopedia

(Difference between revisions)

Revision as of 15:41, 11 September 2015

DISSECTION OF MANNOSYLGLYCERATE SYNTHASE: AN ARCHETYPAL MANNOSYLTRANSFERASE

Structural highlights

2bo4 is a 6 chain structure with sequence from Atcc 43812. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2bo6, 2bo7, 2bo8
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bo4"

@@ Line 2: / Line 2: @@
 <StructureSection load='2bo4' size='340' side='right' caption='[[2bo4]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2bo4]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodothermus_marinus Rhodothermus marinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BO4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BO4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2bo4]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43812 Atcc 43812]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BO4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BO4 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bo6|2bo6]], [[2bo7|2bo7]], [[2bo8|2bo8]]</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=2bo4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bo4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bo4 RCSB], [http://www.ebi.ac.uk/pdbsum/2bo4 PDBsum]</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=2bo4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bo4 OCA], [http://pdbe.org/2bo4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bo4 RCSB], [http://www.ebi.ac.uk/pdbsum/2bo4 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 25: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2bo4" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Rhodothermus marinus]]
+[[Category: Atcc 43812]]
 [[Category: Bolam, D N]]
 [[Category: Davies, G J]]

2bo4

From Proteopedia

Revision as of 15:41, 11 September 2015

DISSECTION OF MANNOSYLGLYCERATE SYNTHASE: AN ARCHETYPAL MANNOSYLTRANSFERASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox