2yjn
From Proteopedia
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| - | [[ | + | ==Structure of the glycosyltransferase EryCIII from the erythromycin biosynthetic pathway, in complex with its activating partner, EryCII== |
| + | <StructureSection load='2yjn' size='340' side='right' caption='[[2yjn]], [[Resolution|resolution]] 3.09Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2yjn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YJN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YJN FirstGlance]. <br> | ||
| + | </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=2yjn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yjn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yjn RCSB], [http://www.ebi.ac.uk/pdbsum/2yjn PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In the biosynthesis of the clinically important antibiotic erythromycin D, the glycosyltransferase (GT) EryCIII, in concert with its partner EryCII, attaches a nucleotide-activated sugar to the macrolide scaffold with high specificity. To understand the role of EryCII, we have determined the crystal structure of the EryCIII.EryCII complex at 3.1 A resolution. The structure reveals a heterotetramer with a distinctive, elongated quaternary organization. The EryCIII subunits form an extensive self-complementary dimer interface at the center of the complex, and the EryCII subunits lie on the periphery. EryCII binds in the vicinity of the putative macrolide binding site of EryCIII but does not make direct interactions with this site. Our biophysical and enzymatic data support a model in which EryCII stabilizes EryCIII and also functions as an allosteric activator of the GT. | ||
| - | + | Structure of the Glycosyltransferase EryCIII in Complex with its Activating P450 Homologue EryCII.,Moncrieffe MC, Fernandez MJ, Spiteller D, Matsumura H, Gay NJ, Luisi BF, Leadlay PF J Mol Biol. 2012 Jan 6;415(1):92-101. Epub 2011 Oct 25. PMID:22056329<ref>PMID:22056329</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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[[Category: Saccharopolyspora erythraea]] | [[Category: Saccharopolyspora erythraea]] | ||
[[Category: Fernandez, M J.]] | [[Category: Fernandez, M J.]] | ||
Revision as of 11:49, 29 October 2014
Structure of the glycosyltransferase EryCIII from the erythromycin biosynthetic pathway, in complex with its activating partner, EryCII
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