4m83: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 1: Line 1:
{{Large structure}}
==Ensemble refinement of protein crystal structure (2IYF) of macrolide glycosyltransferases OleD complexed with UDP and Erythromycin A==
==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]] 1.70&Aring;' scene=''>
<StructureSection load='4m83' size='340' side='right' caption='[[4m83]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== 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>
<table><tr><td colspan='2'>[[4m83]] 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=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>
</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='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='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 "Actinomyces antibioticus" Waksman and Woodruff 1941])</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>
<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://pdbe.org/4m83 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4m83 RCSB], [http://www.ebi.ac.uk/pdbsum/4m83 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4m83 ProSAT]</span></td></tr>
</table>
</table>
{{Large structure}}
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 16: Line 18:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4m83" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
Line 23: Line 26:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Streptomyces antibioticus]]
[[Category: Actinomyces antibioticus waksman and woodruff 1941]]
[[Category: Bingman, C A]]
[[Category: Bingman, C A]]
[[Category: Helmich, K E]]
[[Category: Helmich, K E]]

Revision as of 13:43, 11 August 2016

Warning: this is a large structure, and loading might take a long time or not happen at all.

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

4m83 is a 2 chain structure with sequence from "actinomyces_antibioticus"_waksman_and_woodruff_1941 "actinomyces antibioticus" waksman and woodruff 1941. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Gene:oleD ("Actinomyces antibioticus" Waksman and Woodruff 1941)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT
Warning: this is a large structure, and loading might take a long time or not happen at all.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Bolam DN, Roberts S, Proctor MR, Turkenburg JP, Dodson EJ, Martinez-Fleites C, Yang M, Davis BG, Davies GJ, Gilbert HJ. The crystal structure of two macrolide glycosyltransferases provides a blueprint for host cell antibiotic immunity. Proc Natl Acad Sci U S A. 2007 Mar 27;104(13):5336-41. Epub 2007 Mar 21. PMID:17376874

4m83, resolution 1.70Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=4m83&oldid=2659722"