期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 286, 期 44, 页码 38546-38557出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M111.237602
关键词
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资金
- National Institutes of Health from the Welch Foundation [AI068943, E-1616]
- National Institutes of Health [R01-DC02873]
- U.S. Dept. of Energy, Office of Biological and Environmental Research [DE-AC02-06CH11357]
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 alpha-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.
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