Structure of the C‐terminal domain of Saccharomyces cerevisiae Nup133, a component of the nuclear pore complex
Year: 2011
Type: article
Abstract: Nuclear pore complexes (NPCs), responsible for the nucleo-cytoplasmic exchange of proteins and nucleic acids, are dynamic macromolecular assemblies forming an eight-fold symmetric co-axial ring structure. Yeast (Saccharomyces cerevisiae) NPCs are made up of at least 456 polypeptide chains of ~30 distinct sequences. Many of these components (nucleoporins, Nups) share similar structural motifs and form stable subcomplexes. We have determined a high-resolution crystal structure of the C-terminal domain of yeast Nup133 (ScNup133), a component of the heptameric Nup84 subcomplex. Expression tests yielded ScNup133(944-1157) that produced crystals diffracting to 1.9Å resolution. ScNup133(944-1157) adopts essentially an all α-helical fold, with a short two stranded β-sheet at the C-terminus. The 11 α-helices of ScNup133(944-1157) form a compact fold. In contrast, the previously determined structure of human Nup133(934-1156) bound to a fragment of human Nup107 has its constituent α-helices are arranged in two globular blocks. These differences may reflect structural divergence among homologous nucleoporins.
DOI: 10.1002/prot.22973
Authors: Parthasarathy Sampathkumar, Tarun Gheyi, Stacy A. Miller, Kevin T. Bain, Mark Dickey, Jeffrey B. Bonanno, 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, Andrej Sali, J. Michael Sauder, Stephen K. Burley
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W2149694376