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==Ensemble refinement of protein crystal structure (2IYF) of macrolide glycosyltransferases OleD complexed with UDP and Erythromycin A== | |||
<StructureSection load='4m83' size='340' side='right' caption='[[4m83]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4m83]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_antibioticus Streptomyces antibioticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M83 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M83 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ERY:ERYTHROMYCIN+A'>ERY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2iyf|2iyf]], [[4m60|4m60]], [[4m7p|4m7p]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">oleD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1890 Streptomyces antibioticus])</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=4m83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m83 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m83 RCSB], [http://www.ebi.ac.uk/pdbsum/4m83 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:17376874</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
==See Also== | |||
*[[Glycosyltransferase|Glycosyltransferase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Streptomyces antibioticus]] | [[Category: Streptomyces antibioticus]] | ||
[[Category: Bingman, C A | [[Category: Bingman, C A]] | ||
[[Category: Helmich, K E | [[Category: Helmich, K E]] | ||
[[Category: NatPro, Enzyme Discovery for Natural Product Biosynthesis | [[Category: NatPro, Enzyme Discovery for Natural Product Biosynthesis]] | ||
[[Category: Olmos,, J L | [[Category: Olmos,, J L]] | ||
[[Category: Phillips, G N | [[Category: Phillips, G N]] | ||
[[Category: Singh, S | [[Category: Singh, S]] | ||
[[Category: Thorson, J S | [[Category: Thorson, J S]] | ||
[[Category: Wang, F | [[Category: Wang, F]] | ||
[[Category: Xu, W | [[Category: Xu, W]] | ||
[[Category: Iii, E Martinez | [[Category: Iii, E Martinez]] | ||
[[Category: Enzyme discovery for natural product biosynthesis]] | [[Category: Enzyme discovery for natural product biosynthesis]] | ||
[[Category: Natpro]] | [[Category: Natpro]] | ||
[[Category: Oleandomycin glycosyltransferase]] | [[Category: Oleandomycin glycosyltransferase]] | ||
[[Category: Protein structure initiative]] | [[Category: PSI, Protein structure initiative]] | ||
[[Category: Psi-biology]] | [[Category: Psi-biology]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
[[Category: Transferase-antibiotic complex]] | [[Category: Transferase-antibiotic complex]] | ||
Revision as of 11:28, 5 January 2015
Ensemble refinement of protein crystal structure (2IYF) of macrolide glycosyltransferases OleD complexed with UDP and Erythromycin AEnsemble refinement of protein crystal structure (2IYF) of macrolide glycosyltransferases OleD complexed with UDP and Erythromycin A
Structural highlights
Publication Abstract from PubMedGlycosylation 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Streptomyces antibioticus
- Bingman, C A
- Helmich, K E
- NatPro, Enzyme Discovery for Natural Product Biosynthesis
- Olmos,, J L
- Phillips, G N
- Singh, S
- Thorson, J S
- Wang, F
- Xu, W
- Iii, E Martinez
- Enzyme discovery for natural product biosynthesis
- Natpro
- Oleandomycin glycosyltransferase
- PSI, Protein structure initiative
- Psi-biology
- Structural genomic
- Transferase-antibiotic complex