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J Biol Chem, Vol. 275, Issue 6, 4225-4229, February 11, 2000

Structure of the Influenza C Virus CM2 Protein Transmembrane Domain Obtained by Site-specific Infrared Dichroism and Global Molecular Dynamics Searching^*

Andreas Kukol and Isaiah T. Arkin

From the Cambridge Center for Molecular Recognition, Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, United Kingdom

The 115-residue protein CM2 from Influenza C virus has been recently characterized as a tetrameric integral membrane glycoprotein. Infrared spectroscopy and site-directed infrared dichroism were utilized here to determine its transmembrane structure. The transmembrane domain of CM2 is -helical, and the helices are tilted by  = (14.6 ± 3.0)° from the membrane normal. The rotational pitch angle about the helix axis  for the 1-¹³C-labeled residues Gly⁵⁹ and Leu⁶⁶ is  = (218 ± 17)°, where  is defined as zero for a residue pointing in the direction of the helix tilt. A detailed structure was obtained from a global molecular dynamics search utilizing the orientational data as an energy refinement term. The structure consists of a left-handed coiled-coil with a helix crossing angle of  = 16°. The putative transmembrane pore is occluded by the residue Met⁶⁵. In addition hydrogen/deuterium exchange experiments show that the core is not accessible to water.

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