3Q3H

Crystal structure of the Actinobacillus pleuropneumoniae HMW1C glycosyltransferase in complex with UDP-GLC

Summary for 3Q3H

• Entry DOI: 10.2210/pdb3q3h/pdb
• Related: 3Q3E 3Q3I
• Descriptor: HMW1C-like glycosyltransferase, URIDINE-5'-DIPHOSPHATE, GLYCEROL, ... (4 entities in total)
• Functional Keywords: hmw1c, hmw1, n-glycosylation, transferase
• Biological source: Actinobacillus pleuropneumoniae serovar 1
• Total number of polymer chains: 2
• Total formula weight: 144733.93

Authors

Kawai, F.,Yeo, H.J. (deposition date: 2010-12-21, release date: 2011-08-24, Last modification date: 2024-02-21)

Primary citation

Kawai, F.,Grass, S.,Kim, Y.,Choi, K.J.,St Geme, J.W.,Yeo, H.J.
Structural Insights into the Glycosyltransferase Activity of the Actinobacillus pleuropneumoniae HMW1C-like Protein.
J.Biol.Chem., 286:38546-38557, 2011

PubMed Abstract: Glycosylation of proteins is a fundamental process that influences protein function. The Haemophilus influenzae HMW1 adhesin is an N-linked glycoprotein that mediates adherence to respiratory epithelium, an essential early step in the pathogenesis of H. influenzae disease. HMW1 is glycosylated by HMW1C, a novel glycosyltransferase in the GT41 family that creates N-glycosidic linkages with glucose and galactose at asparagine residues and di-glucose linkages at sites of glucose modification. Here we report the crystal structure of Actinobacillus pleuropneumoniae HMW1C (ApHMW1C), a functional homolog of HMW1C. The structure of ApHMW1C contains an N-terminal all α-domain (AAD) fold and a C-terminal GT-B fold with two Rossmann-like domains and lacks the tetratricopeptide repeat fold characteristic of the GT41 family. The GT-B fold harbors the binding site for UDP-hexose, and the interface of the AAD fold and the GT-B fold forms a unique groove with potential to accommodate the acceptor protein. Structure-based functional analyses demonstrated that the HMW1C protein shares the same structure as ApHMW1C and provided insights into the unique bi-functional activity of HMW1C and ApHMW1C, suggesting an explanation for the similarities and differences of the HMW1C-like proteins compared with other GT41 family members.

PubMed: 21908603
DOI: 10.1074/jbc.M111.237602

Experimental method

X-RAY DIFFRACTION (2.25 Å)