2yjn | pdb_00002yjn

Structure of the glycosyltransferase EryCIII from the erythromycin biosynthetic pathway, in complex with its activating partner, EryCII

spinqualitylabelsall models 2yjn, resolution 3.09Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2yjn is a 2 chain structure with sequence from Sacen. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ERYC3_SACEN] Catalyzes the conversion of alpha-L-mycarosylerythronolide B into erythromycin D in the erythromycin biosynthesis pathway. [ERYC2_SACEN] Involved in the erythromycin biosynthesis pathway. Acts by forming a complex and stabilizing the desosaminyl transferase EryCIII. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glycosyltransferase 3D structures

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