2bo8: Difference between revisions
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|PDB= 2bo8 |SIZE=350|CAPTION= <scene name='initialview01'>2bo8</scene>, resolution 2.80Å | |PDB= 2bo8 |SIZE=350|CAPTION= <scene name='initialview01'>2bo8</scene>, resolution 2.80Å | ||
|SITE= <scene name='pdbsite=AC1:Mn+Binding+Site+For+Chain+J'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Mn+Binding+Site+For+Chain+J'>AC1</scene> | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GDX:GUANOSINE+5'-(TRIHYDROGEN+DIPHOSPHATE),+P'-D-MANNOPYRANOSYL+ESTER'>GDX</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bo8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bo8 OCA], [http://www.ebi.ac.uk/pdbsum/2bo8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bo8 RCSB]</span> | |||
}} | }} | ||
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[[Category: Taylor, E.]] | [[Category: Taylor, E.]] | ||
[[Category: Yang, M.]] | [[Category: Yang, M.]] | ||
[[Category: catalysis]] | [[Category: catalysis]] | ||
[[Category: glycosyltransferase]] | [[Category: glycosyltransferase]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:09:18 2008'' | ||
Revision as of 23:09, 30 March 2008
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| 2bo8, resolution 2.80Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | CL, GDX, MN | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
DISSECTION OF MANNOSYLGLYCERATE SYNTHASE: AN ARCHETYPAL MANNOSYLTRANSFERASE
Overview
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.
About this Structure
2BO8 is a Single protein structure of sequence from Rhodothermus marinus. Full crystallographic information is available from OCA.
Reference
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
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