2YJN

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

2YJN の概要

• エントリーDOI: 10.2210/pdb2yjn/pdb
• 分子名称: GLYCOSYLTRANSFERASE, DTDP-4-KETO-6-DEOXY-HEXOSE 3,4-ISOMERASE (2 entities in total)
• 機能のキーワード: transferase, cytochrome p450
• 由来する生物種: SACCHAROPOLYSPORA ERYTHRAEA; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 88874.18

構造登録者

Moncrieffe, M.C.,Fernandez, M.J.,Spiteller, D.,Matsumura, H.,Gay, N.J.,Luisi, B.F.,Leadlay, P.F. (登録日: 2011-05-20, 公開日: 2011-11-09, 最終更新日: 2024-05-08)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.091 Å)