2iya: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
== | |||
==The crystal structure of macrolide glycosyltransferases: A blueprint for antibiotic engineering== | |||
<StructureSection load='2iya' size='340' side='right' caption='[[2iya]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='2iya' size='340' side='right' caption='[[2iya]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2iya]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_antibioticus"_waksman_and_woodruff_1941 "actinomyces antibioticus" waksman and woodruff 1941]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IYA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IYA FirstGlance]. <br> | <table><tr><td colspan='2'>[[2iya]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_antibioticus"_waksman_and_woodruff_1941 "actinomyces antibioticus" waksman and woodruff 1941]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IYA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IYA FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene>, <scene name='pdbligand=ZIO:(3S,5R,6S,7R,8R,11R,12S,13R,14S,15S)-6-HYDROXY-5,7,8,11,13,15-HEXAMETHYL-4,10-DIOXO-14-{[3,4,6-TRIDEOXY-3-(DIMETHYLAMINO)-BETA-D-XYLO-HEXOPYRANOSYL]OXY}-1,9-DIOXASPIRO[2.13]HEXADEC-12-YL+2,6-DIDEOXY-3-O-METHYL-ALPHA-L-ARABINO-HEXOPYRANOSIDE'>ZIO</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene>, <scene name='pdbligand=ZIO:(3S,5R,6S,7R,8R,11R,12S,13R,14S,15S)-6-HYDROXY-5,7,8,11,13,15-HEXAMETHYL-4,10-DIOXO-14-{[3,4,6-TRIDEOXY-3-(DIMETHYLAMINO)-BETA-D-XYLO-HEXOPYRANOSYL]OXY}-1,9-DIOXASPIRO[2.13]HEXADEC-12-YL+2,6-DIDEOXY-3-O-METHYL-ALPHA-L-ARABINO-HEXOPYRANOSIDE'>ZIO</scene></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=2iya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iya OCA], [http://pdbe.org/2iya PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2iya RCSB], [http://www.ebi.ac.uk/pdbsum/2iya PDBsum]</span></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=2iya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iya OCA], [http://pdbe.org/2iya PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2iya RCSB], [http://www.ebi.ac.uk/pdbsum/2iya PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2iya ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 10: | Line 11: | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iy/2iya_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iy/2iya_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
| Line 25: | Line 26: | ||
</div> | </div> | ||
<div class="pdbe-citations 2iya" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2iya" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 21:52, 24 January 2018
The crystal structure of macrolide glycosyltransferases: A blueprint for antibiotic engineeringThe crystal structure of macrolide glycosyltransferases: A blueprint for antibiotic engineering
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. 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. References
|
| ||||||||||||||||