2YJN

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

Summary for 2YJN

• Entry DOI: 10.2210/pdb2yjn/pdb
• Descriptor: GLYCOSYLTRANSFERASE, DTDP-4-KETO-6-DEOXY-HEXOSE 3,4-ISOMERASE (2 entities in total)
• Functional Keywords: transferase, cytochrome p450
• Biological source: SACCHAROPOLYSPORA ERYTHRAEA; More
• Total number of polymer chains: 2
• Total formula weight: 88874.18

Authors

Moncrieffe, M.C.,Fernandez, M.J.,Spiteller, D.,Matsumura, H.,Gay, N.J.,Luisi, B.F.,Leadlay, P.F. (deposition date: 2011-05-20, release date: 2011-11-09, Last modification date: 2024-05-08)

Primary citation

Moncrieffe, M.C.,Fernandez, M.,Spiteller, D.,Matsumura, H.,Gay, N.J.,Luisi, B.F.,Leadlay, P.F.
Structure of the Glycosyltransferase Eryciii in Complex with its Activating P450 Homologue Erycii.
J.Mol.Biol., 415:92-, 2012

PubMed Abstract: 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 Å 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.

PubMed: 22056329
DOI: 10.1016/J.JMB.2011.10.036

Experimental method

X-RAY DIFFRACTION (3.091 Å)