J Michael Sauder - Structures of the autoproteolytic domain from the Saccharomyces cerevisiae nuclear pore complex component, Nup145

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  Publication Details (including relevant citation   information):

  Proteins (2010) 78: 1992-1998.

  Parthasarathy Sampathkumar, Sinem A. Ozyurt, Johnny Do, Kevin T.   Bain, Mark Dickey, Logan A. Rodgers, Tarun Gheyi, Andrej Sali,   Seung Joong Kim, Jeremy Phillips, Ursula Pieper, Javier   Fernandez-Martinez, Josef D. Franke, Anne Martel, Hiro Tsuruta,   Shane Atwell, Devon A. Thompson, J. Spencer Emtage, Stephen R.   Wasserman, Michael P. Rout, J. Michael Sauder, Stephen K. Burley


  As a part of ongoing efforts at the New York SGX Research Center   for  Structural Genomics (www.nysgxrc.org)  to determine crystal   structures of distinct components of the yeast  nuclear pore   complex (NPC), we report herein structures of Nup145N residues   443-605  [Nup145N(443-605)] from the larger autoproteolytic   segment. The  monomeric architecture of Nup145N(443-605) is   similar to that of the  autoproteolytic domain of human   Nup98-N and the homologous domain of  Nup116. In contrast,   Nup145N(443-605) and Nup98-N show different modes  of   association in the crystalline state. Results of Small Angle   X-ray  Scattering (SAXS) in solution are consistent with the   head-to-tail dimer  of Nup145N(443-605), observed in two   different crystal forms.

  Address (URL): http://www3.interscience.wiley.com/journal/123305952/abstract