2bo6
From Proteopedia
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| - | [[Image:2bo6.gif|left|200px]]<br /><applet load="2bo6" size=" | + | [[Image:2bo6.gif|left|200px]]<br /><applet load="2bo6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2bo6, resolution 2.45Å" /> | caption="2bo6, resolution 2.45Å" /> | ||
'''DISSECTION OF MANNOSYLGLYCERATE SYNTHASE: AN ARCHETYPAL MANNOSYLTRANSFERASE'''<br /> | '''DISSECTION OF MANNOSYLGLYCERATE SYNTHASE: AN ARCHETYPAL MANNOSYLTRANSFERASE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BO6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodothermus_marinus Rhodothermus marinus] with MN and DGY as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Mn Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2BO6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodothermus_marinus Rhodothermus marinus] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=DGY:'>DGY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Mn+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BO6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:26:14 2008'' |
Revision as of 08:26, 3 February 2008
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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
2BO6 is a Single protein structure of sequence from Rhodothermus marinus with and as ligands. Known structural/functional Site: . 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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