1QU1

CRYSTAL STRUCTURE OF EHA2 (23-185)

Summary for 1QU1

• Entry DOI: 10.2210/pdb1qu1/pdb
• Descriptor: PROTEIN (INFLUENZA RECOMBINANT HA2 CHAIN) (2 entities in total)
• Functional Keywords: hemagglutinin, low-ph, virus/viral protein, viral protein
• Biological source: Influenza A virus
• Cellular location: Virion membrane; Single-pass type I membrane protein (Potential): P03437
• Total number of polymer chains: 6
• Total formula weight: 108366.04

Authors

Chen, J.,Skehel, J.J.,Wiley, D.C. (deposition date: 1999-07-05, release date: 2000-01-05, Last modification date: 2024-10-16)

Primary citation

Chen, J.,Skehel, J.J.,Wiley, D.C.
N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coil.
Proc.Natl.Acad.Sci.USA, 96:8967-8972, 1999

PubMed Abstract: The structure of a stable recombinant ectodomain of influenza hemagglutinin HA(2) subunit, EHA(2) (23-185), defined by proteolysis studies of the intact bacterial-expressed ectodomain, was determined to 1.9-A resolution by using x-ray crystallography. The structure reveals a domain composed of N- and C-terminal residues that form an N cap terminating both the N-terminal alpha-helix and the central coiled coil. The N cap is formed by a conserved sequence, and part of it is found in the neutral pH conformation of HA. The C-terminal 23 residues of the ectodomain form a 72-A long nonhelical structure ordered to within 7 residues of the transmembrane anchor. The structure implies that continuous alpha helices are not required for membrane fusion at either the N or C termini. The difference in stability between recombinant molecules with and without the N cap sequences suggests that additional free energy for membrane fusion may become available after the formation of the central triple-stranded coiled coil and insertion of the fusion peptide into the target membrane.

PubMed: 10430879
DOI: 10.1073/pnas.96.16.8967

Experimental method

X-RAY DIFFRACTION (1.9 Å)