1FLC

X-RAY STRUCTURE OF THE HAEMAGGLUTININ-ESTERASE-FUSION GLYCOPROTEIN OF INFLUENZA C VIRUS

1FLC の概要

• エントリーDOI: 10.2210/pdb1flc/pdb
• 分子名称: HAEMAGGLUTININ-ESTERASE-FUSION GLYCOPROTEIN, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: esterase, receptor binding, membrane fusion, virus, influenza, hydrolase
• 由来する生物種: Influenza C virus (C/Johannesburg/1/66); 詳細
• 細胞内の位置: Virion membrane ; Single-pass type I membrane protein : P07975
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 210422.85

構造登録者

Rosenthal, P.B.,Zhang, X.,Formanowski, F.,Fitz, W.,Wong, C.H.,Meier-Ewert, H.,Skehel, J.J.,Wiley, D.C. (登録日: 1999-02-22, 公開日: 2000-03-01, 最終更新日: 2024-11-06)

主引用文献

Rosenthal, P.B.,Zhang, X.
Structure of the haemagglutinin-esterase-fusion glycoprotein of influenza C virus.
Nature, 396:92-96, 1998

PubMed Abstract: The spike glycoproteins of the lipid-enveloped orthomyxoviruses and paramyxoviruses have three functions: to recognize the receptor on the cell surface, to mediate viral fusion with the cell membrane, and to destroy the receptor. In influenza C virus, a single glycoprotein, the haemagglutinin-esterase-fusion (HEF) protein, possesses all three functions. In influenza A and B, the first two activities are mediated by haemagglutinin and the third by a second glycoprotein, neuraminidase. Here we report the crystal structure of the HEF envelope glycoprotein of influenza C virus. We have identified the receptor-binding site and the receptor-destroying enzyme (9-O-acetylesterase) sites, by using receptor analogues. The receptor-binding domain is structurally similar to the sialic acid-binding domain of influenza A haemagglutinin, but binds 9-O-acetylsialic acid. The esterase domain has a structure similar to the esterase from Streptomyces scabies and a brain acetylhydrolase. The receptor domain is inserted into a surface loop of the esterase domain and the esterase domain is inserted into a surface loop of the stem. The stem domain is similar to that of influenza A haemagglutinin, except that the triple-stranded, alpha-helical bundle diverges at both of its ends, and the amino terminus of HEF2, the fusion peptide, is partially exposed. The segregation of HEF's three functions into structurally distinct domains suggests that the entire stem region, including sequences at the amino and carboxy termini of HEF1 which precede the post-translational cleavage site between HEF1 and HEF2, forms an independent fusion domain which is probably derived from an ancestral membrane fusion protein.

PubMed: 9817207
DOI: 10.1038/23974

実験手法

X-RAY DIFFRACTION (3.2 Å)