3KFO

Crystal structure of the C-terminal domain from the nuclear pore complex component NUP133 from Saccharomyces cerevisiae

Summary for 3KFO

• Entry DOI: 10.2210/pdb3kfo/pdb
• Descriptor: Nucleoporin NUP133, GLYCEROL (3 entities in total)
• Functional Keywords: nuclear pore complex, nup133, yeast, proteolysis, structural genomics, psi2, protein structure initiative, new york structural genomix research consortium, nysgxrc, membrane, mrna transport, nucleus, phosphoprotein, protein transport, translocation, transport, new york sgx research center for structural genomics
• Biological source: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast)
• Total number of polymer chains: 1
• Total formula weight: 33335.22

Authors

Sampathkumar, P.,Bonanno, J.B.,Miller, S.,Bain, K.,Dickey, M.,Gheyi, T.,Almo, S.C.,Rout, M.,Sali, A.,Phillips, J.,Pieper, U.,Fernandez-Martinez, J.,Franke, J.D.,Atwell, S.,Thompson, D.A.,Emtage, J.S.,Wasserman, S.,Sauder, J.M.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2009-10-27, release date: 2010-01-26, Last modification date: 2024-11-06)

Primary citation

Sampathkumar, P.,Gheyi, T.,Miller, S.A.,Bain, K.T.,Dickey, M.,Bonanno, J.B.,Kim, S.J.,Phillips, J.,Pieper, U.,Fernandez-Martinez, J.,Franke, J.D.,Martel, A.,Tsuruta, H.,Atwell, S.,Thompson, D.A.,Emtage, J.S.,Wasserman, S.R.,Rout, M.P.,Sali, A.,Sauder, J.M.,Burley, S.K.
Structure of the C-terminal domain of Saccharomyces cerevisiae Nup133, a component of the nuclear pore complex.
Proteins, 79:1672-1677, 2011

PubMed 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 () 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.

PubMed: 21365675
DOI: 10.1002/prot.22973

Experimental method

X-RAY DIFFRACTION (1.9 Å)