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X-ray crystallographic determination of the structure of the influenza c virus haemagglutinin-esterase-fusion glycoprotein

Academic Article
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Overview

authors

  • Zhang, X. D.
  • Rosenthal, P. B.
  • Formanowski, F.
  • Fitz, W.
  • Wong, Chi-Huey
  • Meier-Ewert, H.
  • Skehel, J. J.
  • Wiley, D. C.

publication date

  • May 1999

journal

  • Acta Crystallographica Section D-Biological Crystallography  Journal

abstract

  • The structure of the haemagglutinin-esterase-fusion (HEF) glycoprotein from influenza C virus has been determined to 3.2 A resolution by X-ray crystallography. A synthetic mercury-containing esterase inhibitor and receptor analogue, 9-acetamidosialic acid alpha-thiomethylmercuryglycoside, was designed as the single isomorphous heavy-atom derivative. The asymmetric unit of one crystal form (form I; P4322, a = b = 155.4, c = 414.4 A) contained an HEF trimer. Six mercury sites identifying the three haemagglutination and three esterase sites were located by difference Patterson map analysis of a 6.5 A resolution derivative data set. These positions defined the molecular threefold-symmetry axis of the HEF trimer. A molecular envelope was defined by averaging a 7.0 A resolution electron-density map, phased by single isomorphous replacement (SIR), about the non-crystallographic threefold-symmetry axis. Iterative non-crystallographic symmetry averaging in real space, solvent flattening and histogram matching were used to extend the phases to 3.5 A resolution. Molecular replacement of the model into a second crystal form (form II; P43212, a = b = 217.4, c = 421.4 A) containing two HEF trimers per asymmetric unit permitted iterative ninefold averaging of the electron density. The 3.5 A electron-density map allowed an unambiguous tracing of the polypeptide chain and identification of N-linked carbohydrates. The model has been refined by least squares to 3.2 A resolution (Rfree = 26.7%).

subject areas

  • Acetylesterase
  • Binding Sites
  • Crystallography, X-Ray
  • Glycoproteins
  • Hemagglutinins, Viral
  • Influenzavirus C
  • Mercury
  • Models, Molecular
  • Protein Conformation
  • Viral Fusion Proteins
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Identity

International Standard Serial Number (ISSN)

  • 0907-4449

Digital Object Identifier (DOI)

  • 10.1107/s0907444999000232

PubMed ID

  • 10216291
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Additional Document Info

start page

  • 945

end page

  • 961

volume

  • 55

issue

  • Pt 5

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