2iyf
From Proteopedia
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| - | [[Image:2iyf.gif|left|200px]]<br /><applet load="2iyf" size=" | + | [[Image:2iyf.gif|left|200px]]<br /><applet load="2iyf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2iyf, resolution 1.70Å" /> | caption="2iyf, resolution 1.70Å" /> | ||
'''THE CRYSTAL STRUCTURE OF MACROLIDE GLYCOSYLTRANSFERASES: A BLUEPRINT FOR ANTIBIOTIC ENGINEERING'''<br /> | '''THE CRYSTAL STRUCTURE OF MACROLIDE GLYCOSYLTRANSFERASES: A BLUEPRINT FOR ANTIBIOTIC ENGINEERING'''<br /> | ||
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| + | ==Overview== | ||
| + | Glycosylation of macrolide antibiotics confers host cell immunity from, endogenous and exogenous agents. The Streptomyces antibioticus, glycosyltransferases, OleI and OleD, glycosylate and inactivate, oleandomycin and diverse macrolides including erythromycin, respectively., The structure of these enzyme-ligand complexes, in tandem with kinetic, analysis of site-directed variants, provide insight into the interaction, of macrolides with their synthetic apparatus. Erythromycin binds to OleD, and the 23S RNA of its target ribosome in the same conformation and, although the antibiotic contains a large number of polar groups, its, interaction with these macromolecules is primarily through hydrophobic, contacts. Erythromycin and oleandomycin, when bound to OleD and OleI, respectively, adopt different conformations, reflecting a subtle effect on, sugar positioning by virtue of a single change in the macrolide backbone., The data reported here provide structural insight into the mechanism of, resistance to both endogenous and exogenous antibiotics, and will provide, a platform for the future redesign of these catalysts for antibiotic, remodelling. | ||
==About this Structure== | ==About this Structure== | ||
| - | 2IYF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_antibioticus Streptomyces antibioticus] with ERY, MG and UDP as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional | + | 2IYF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_antibioticus Streptomyces antibioticus] with <scene name='pdbligand=ERY:'>ERY</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=UDP:'>UDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Ery Binding Site For Residue A 1400'>AC1</scene>, <scene name='pdbsite=AC2:Udp Binding Site For Residue A 1401'>AC2</scene>, <scene name='pdbsite=AC3:Ery Binding Site For Residue B 1399'>AC3</scene>, <scene name='pdbsite=AC4:Udp Binding Site For Residue B 1400'>AC4</scene> and <scene name='pdbsite=AC5:Mg Binding Site For Residue B 1401'>AC5</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IYF OCA]. |
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| + | ==Reference== | ||
| + | The crystal structure of two macrolide glycosyltransferases provides a blueprint for host cell antibiotic immunity., Bolam DN, Roberts S, Proctor MR, Turkenburg JP, Dodson EJ, Martinez-Fleites C, Yang M, Davis BG, Davies GJ, Gilbert HJ, Proc Natl Acad Sci U S A. 2007 Mar 27;104(13):5336-41. Epub 2007 Mar 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17376874 17376874] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces antibioticus]] | [[Category: Streptomyces antibioticus]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 31 10:57:14 2008'' |
Revision as of 08:57, 31 January 2008
|
THE CRYSTAL STRUCTURE OF MACROLIDE GLYCOSYLTRANSFERASES: A BLUEPRINT FOR ANTIBIOTIC ENGINEERING
Overview
Glycosylation of macrolide antibiotics confers host cell immunity from, endogenous and exogenous agents. The Streptomyces antibioticus, glycosyltransferases, OleI and OleD, glycosylate and inactivate, oleandomycin and diverse macrolides including erythromycin, respectively., The structure of these enzyme-ligand complexes, in tandem with kinetic, analysis of site-directed variants, provide insight into the interaction, of macrolides with their synthetic apparatus. Erythromycin binds to OleD, and the 23S RNA of its target ribosome in the same conformation and, although the antibiotic contains a large number of polar groups, its, interaction with these macromolecules is primarily through hydrophobic, contacts. Erythromycin and oleandomycin, when bound to OleD and OleI, respectively, adopt different conformations, reflecting a subtle effect on, sugar positioning by virtue of a single change in the macrolide backbone., The data reported here provide structural insight into the mechanism of, resistance to both endogenous and exogenous antibiotics, and will provide, a platform for the future redesign of these catalysts for antibiotic, remodelling.
About this Structure
2IYF is a Single protein structure of sequence from Streptomyces antibioticus with , and as ligands. Known structural/functional Sites: , , , and . Full crystallographic information is available from OCA.
Reference
The crystal structure of two macrolide glycosyltransferases provides a blueprint for host cell antibiotic immunity., Bolam DN, Roberts S, Proctor MR, Turkenburg JP, Dodson EJ, Martinez-Fleites C, Yang M, Davis BG, Davies GJ, Gilbert HJ, Proc Natl Acad Sci U S A. 2007 Mar 27;104(13):5336-41. Epub 2007 Mar 21. PMID:17376874
Page seeded by OCA on Thu Jan 31 10:57:14 2008
Categories: Single protein | Streptomyces antibioticus | Bolam, D.N. | Davies, G.J. | Davis, B.G. | Dodson, E.J. | Gilbert, H.J. | Martinez-Fleites, C. | Proctor, M.R. | Roberts, S.M. | Turkenburg, J.P. | Yang, M. | ERY | MG | UDP | Antibiotic resistance | Carbohydrate | Enzyme | Glycosylation | Glycosyltransferase | Macrolide | Transferase
