NMR structure of the mengovirus Leader protein zinc-finger domain.
The Leader protein is a defining feature of picornaviruses from the Cardiovirus genus. This protein was recently shown to inhibit cellular nucleocytoplasmic transport through an activity mapped to its zinc-binding region. Here we report the three-dimensional solution structure determined by nuclear magnetic resonance (NMR) spectroscopy of this domain (residues 5-28) from mengovirus. The domain forms a CHCC zinc-finger with a fold comprising a beta-hairpin followed by a short alpha-helix that can adopt two different conformations. This structure is divergent from those of other eukaryotic zinc-fingers and instead resembles motifs found in a group of DNA-binding proteins from Archaea.
Cornilescu
Claudia C
CC
Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706-1544, USA. cclaudia@nmrfam.wisc.edu <cclaudia@nmrfam.wisc.edu>
Porter
Frederick W
FW
Zhao
Kate Qin
KQ
Palmenberg
Ann C
AC
Markley
John L
JL
D000595:Amino Acid Sequence; D008574:Mengovirus; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017361:Viral Nonstructural Proteins / Q000737:chemistry*; D016335:Zinc Fingers
D017361:Viral Nonstructural Proteins