5HEC

CgT structure in dimer

5HEC の概要

• エントリーDOI: 10.2210/pdb5hec/pdb
• 関連するPDBエントリー: 5HEA
• 分子名称: Putative glycosyltransferase (GalT1) (2 entities in total)
• 機能のキーワード: glycosyltransferase, helix binding domain, transferase
• 由来する生物種: Streptococcus parasanguinis FW213
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68589.29

構造登録者

Zhang, H.,Wu, H. (登録日: 2016-01-05, 公開日: 2016-08-31, 最終更新日: 2024-10-09)

主引用文献

Zhang, H.,Zhou, M.,Yang, T.,Haslam, S.M.,Dell, A.,Wu, H.
New Helical Binding Domain Mediates a Glycosyltransferase Activity of a Bifunctional Protein.
J.Biol.Chem., 291:22106-22117, 2016

PubMed Abstract: Serine-rich repeat glycoproteins (SRRPs) conserved in streptococci and staphylococci are important for bacterial colonization and pathogenesis. Fap1, a well studied SRRP is a major surface constituent of Streptococcus parasanguinis and is required for bacterial adhesion and biofilm formation. Biogenesis of Fap1 is a multistep process that involves both glycosylation and secretion. A series of glycosyltransferases catalyze sequential glycosylation of Fap1. We have identified a unique hybrid protein dGT1 (dual glycosyltransferase 1) that contains two distinct domains. N-terminal DUF1792 is a novel GT-D-type glycosyltransferase, transferring Glc residues to Glc-GlcNAc-modified Fap1. C-terminal dGT1 (CgT) is predicted to possess a typical GT-A-type glycosyltransferase, however, the activity remains unknown. In this study, we determine that CgT is a distinct glycosyltransferase, transferring GlcNAc residues to Glc-Glc-GlcNAc-modified Fap1. A 2.4-Å x-ray crystal structure reveals that CgT has a unique binding domain consisting of three α helices in addition to a typical GT-A-type glycosyltransferase domain. The helical domain is crucial for the oligomerization of CgT. Structural and biochemical studies revealed that the helix domain is required for the protein-protein interaction and crucial for the glycosyltransferase activity of CgT in vitro and in vivo As the helix domain presents a novel structural fold, we conclude that CgT represents a new member of GT-A-type glycosyltransferases.

PubMed: 27539847
DOI: 10.1074/jbc.M116.731695

実験手法

X-RAY DIFFRACTION (2.395 Å)