Crystallization and preliminary X-ray crystallographic analysis of importin-? from Neurospora crassa.

ABSTRACT: Importin-? recognizes cargo proteins that contain classical nuclear localization sequences (NLS) and, in complex with importin-?, is able to translocate nuclear proteins through the nuclear pore complex. The filamentous fungus Neurospora crassa is a well studied organism that has been widely used as a model organism for fundamental aspects of eukaryotic biology, and is important for understanding the specific mechanisms of protein transport to the cell nucleus. In this work, the crystallization and preliminary X-ray diffraction analysis of importin-? from N. crassa (IMP?-Nc) complexed with a classical NLS peptide (SV40 NLS) are reported. IMP?-Nc-SV40 NLS crystals diffracted X-rays to 2.0?Å resolution and the structure was solved by molecular-replacement techniques, leading to a monomeric structure. The observation of the electron-density map indicated the presence of SV40 NLSs interacting at both the minor and major NLS-binding sites of the protein.

SUBMITTER: Bernardes NE 

PROVIDER: S-EPMC3976073 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature