Structures of the autoproteolytic domain from the Saccharomyces cerevisiae nuclear pore complex component, Nup145 - PubMed (original) (raw)

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

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Structures of the autoproteolytic domain from the Saccharomyces cerevisiae nuclear pore complex component, Nup145

Parthasarathy Sampathkumar et al. Proteins. 2010 Jun.

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Figures

Figure 1

Figure 1

A: Schematic representation of the S. cerevisiae Nup145 protein. The “FG” repeats are shaded in blue and the expression construct boundaries of Nup145N(443–605) delimited in gray. The site of autoproteolysis is marked with a red triangle. B: Stereoview of the Nup145N(443–605) monomer. Cartoon of Chain B is shown as a rainbow from blue to red from N- to C-terminus. C: Stereoview of the Nup145N(443–605) head-to-tail dimer seen in the tetragonal crystals. Cartoons of Chains A and B are shown in grey and green, respectively. Residues involved in dimeric interactions from Chain B are colored in blue and those from Chain A are colored in red. D: Stereoview of the superposition of Nup145N(443–605) dimers from two different crystal forms. Nup145N(443–605) forms an identical dimer in both tetragonal and hexagonal crystal forms. All structural superpositions were carried out using SSM. The A and B chains of tetragonal form are shown as gray and green ribbons, respectively. Similarly, A and B chains of the hexagonal forms are shown in yellow and wheat, respectively.

Figure 2

Figure 2

A: Analytical gel filtration profile of Nup145N(443–605) at concentrations of 11.8 (black), 22.7 (blue), and 46.0mg/ml (red) with elution times 21.5, 21.3, and 21.1min, respectively. B: Comparison of the merged experimental SAXS profile (red) of Nup145N(443–605) with SAXS profiles computed by IMP for the crystallographic dimer (blue) and monomer (green) structures (inset shows the SAXS profiles across the entire measured resolution range). C: The shape of Nup145N(443–605) represented as mesh derived from the experimental SAXS profile.

Figure 3

Figure 3

A: Stereoview of Nup145N(443–605, green) superposed on a representative NMR structure of Nup116 (PDB Code 2AIV; grey). B: Stereoview of the Nup145N(443–605, chain B; green) superposed on Nup98-N (grey) from the Nup98-N:C-terminal fragment complex (PDB Code 2Q5Y). C: Stereoview of the dimeric association of Nup98-N in the Nup98-N:C-terminal fragment complex. The ordered C-terminal fragment tri-peptides are shown in magenta. Residues contributing to the dimer interface from the A and C chains are colored blue and orange, respectively. The N- and C-terminal residues are shown on the cartoons as blue and red spheres, respectively.

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