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Structure of the C‐terminal domain of Saccharomyces cerevisiae Nup133, a component of the nuclear pore complex
Author(s) -
Sampathkumar Parthasarathy,
Gheyi Tarun,
Miller Stacy A.,
Bain Kevin T.,
Dickey Mark,
Bonanno Jeffrey B.,
Kim Seung Joong,
Phillips Jeremy,
Pieper Ursula,
FernandezMartinez Javier,
Franke Josef D.,
Martel Anne,
Tsuruta Hiro,
Atwell Shane,
Thompson Devon A.,
Emtage J. Spencer,
Wasserman Stephen R.,
Rout Michael P.,
Sali Andrej,
Sauder J. Michael,
Burley Stephen K.
Publication year - 2011
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.22973
Subject(s) - library science , structural genomics , management , engineering , computer science , biology , biochemistry , protein structure , economics
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 {approx}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 1.9{angstrom} resolution. ScNup133(944-1157) adopts essentially an all {alpha}-helical fold, with a short two stranded {beta}-sheet at the C-terminus. The 11 {alpha}-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 {alpha}-helices are arranged in two globular blocks. These differences may reflect structural divergence among homologous nucleoporins.