2iyf

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[[Image:2iyf.gif|left|200px]]
 
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==The crystal structure of macrolide glycosyltransferases: A blueprint for antibiotic engineering==
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The line below this paragraph, containing "STRUCTURE_2iyf", creates the "Structure Box" on the page.
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<StructureSection load='2iyf' size='340' side='right'caption='[[2iyf]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2iyf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_antibioticus Streptomyces antibioticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IYF FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
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{{STRUCTURE_2iyf| PDB=2iyf | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2iyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iyf OCA], [https://pdbe.org/2iyf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iyf RCSB], [https://www.ebi.ac.uk/pdbsum/2iyf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iyf ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/OLED_STRAT OLED_STRAT] Specifically inactivates oleandomycin via 2'-O-glycosylation using UDP-glucose.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iy/2iyf_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2iyf ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''THE CRYSTAL STRUCTURE OF MACROLIDE GLYCOSYLTRANSFERASES: A BLUEPRINT FOR ANTIBIOTIC ENGINEERING'''
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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>
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==Overview==
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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.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2IYF is a [[Single protein]] structure of 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=2IYF OCA].
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</div>
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<div class="pdbe-citations 2iyf" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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://www.ncbi.nlm.nih.gov/pubmed/17376874 17376874]
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*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
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[[Category: Single protein]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Streptomyces antibioticus]]
[[Category: Streptomyces antibioticus]]
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[[Category: Bolam, D N.]]
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[[Category: Bolam DN]]
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[[Category: Davies, G J.]]
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[[Category: Davies GJ]]
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[[Category: Davis, B G.]]
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[[Category: Davis BG]]
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[[Category: Dodson, E J.]]
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[[Category: Dodson EJ]]
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[[Category: Gilbert, H J.]]
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[[Category: Gilbert HJ]]
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[[Category: Martinez-Fleites, C.]]
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[[Category: Martinez-Fleites C]]
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[[Category: Proctor, M R.]]
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[[Category: Proctor MR]]
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[[Category: Roberts, S M.]]
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[[Category: Roberts SM]]
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[[Category: Turkenburg, J P.]]
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[[Category: Turkenburg JP]]
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[[Category: Yang, M.]]
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[[Category: Yang M]]
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[[Category: Antibiotic resistance]]
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[[Category: Carbohydrate]]
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[[Category: Enzyme]]
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[[Category: Glycosylation]]
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[[Category: Glycosyltransferase]]
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[[Category: Macrolide]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:04:47 2008''
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Current revision

The crystal structure of macrolide glycosyltransferases: A blueprint for antibiotic engineering

PDB ID 2iyf

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