1BYU

CANINE GDP-RAN

Summary for 1BYU

• Entry DOI: 10.2210/pdb1byu/pdb
• Descriptor: PROTEIN (GTP-BINDING PROTEIN RAN), MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: gtpase, nuclear transport, transport protein
• Biological source: Canis lupus familiaris (dog)
• Cellular location: Nucleus: P62825
• Total number of polymer chains: 2
• Total formula weight: 49899.30

Authors

Stewart, M.,Kent, H.M.,Mccoy, A.J. (deposition date: 1998-10-18, release date: 1998-12-02, Last modification date: 2024-04-03)

Primary citation

Stewart, M.,Kent, H.M.,McCoy, A.J.
The structure of the Q69L mutant of GDP-Ran shows a major conformational change in the switch II loop that accounts for its failure to bind nuclear transport factor 2 (NTF2).
J.Mol.Biol., 284:1517-1527, 1998

PubMed Abstract: We report the 2.3 A resolution X-ray crystal structure of the GDP-bound form of the RanQ69L mutant that is used extensively in studies of nucleocytoplasmic transport and cell-cycle progression. When the structure of GDP-RanQ69L from monoclinic crystals with P21 symmetry was compared with the structure of wild-type Ran obtained from monoclinic crystals, the Q69L mutant showed a large conformational change in residues 68-74, which are in the switch II region of the molecule which changes conformation in response to nucleotide state and which forms the major interaction interface with nuclear transport factor 2 (NTF2, sometimes called p10). This conformational change alters the positions of key residues such as Lys71, Phe72 and Arg76 that are crucial for the interaction of GDP-Ran with NTF2 and indeed, solution binding studies were unable to detect any interaction between NTF2 and GDP-RanQ69L under conditions where GDP-Ran bound effectively. This interaction between NTF2 and GDP-Ran is required for efficient nuclear protein import and may function between the docking and translocation steps of the pathway.

PubMed: 9878368
DOI: 10.1006/jmbi.1998.2204

Experimental method

X-RAY DIFFRACTION (2.15 Å)