1I2M

RAN-RCC1-SO4 COMPLEX

Summary for 1I2M

• Entry DOI: 10.2210/pdb1i2m/pdb
• Related: 1BYU 1RRP 1a12
• Descriptor: GTP-BINDING NUCLEAR PROTEIN RAN, REGULATOR OF CHROMOSOME CONDENSATION 1, SULFATE ION, ... (4 entities in total)
• Functional Keywords: beta-propeller, g fold or gtpase fold, cell cycle
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus : P62826 P18754
• Total number of polymer chains: 4
• Total formula weight: 134939.14

Authors

Renault, L.,Kuhlmann, J.,Henkel, A.,Wittinghofer, A. (deposition date: 2001-02-11, release date: 2001-05-02, Last modification date: 2023-08-09)

Primary citation

Renault, L.,Kuhlmann, J.,Henkel, A.,Wittinghofer, A.
Structural basis for guanine nucleotide exchange on Ran by the regulator of chromosome condensation (RCC1).
Cell(Cambridge,Mass.), 105:245-255, 2001

PubMed Abstract: RCC1 (regulator of chromosome condensation), a beta propeller chromatin-bound protein, is the guanine nucleotide exchange factor (GEF) for the nuclear GTP binding protein Ran. We report here the 1.8 A crystal structure of a Ran*RCC1 complex in the absence of nucleotide, an intermediate in the multistep GEF reaction. In contrast to previous structures, the phosphate binding region of the nucleotide binding site is perturbed only marginally, possibly due to the presence of a polyvalent anion in the P loop. Biochemical experiments show that a sulfate ion stabilizes the Ran*RCC1 complex and inhibits dissociation by guanine nucleotides. Based on the available structural and biochemical evidence, we present a unified scenario for the GEF mechanism where interaction of the P loop lysine with an acidic residue is a crucial element for the overall reaction.

PubMed: 11336674
DOI: 10.1016/S0092-8674(01)00315-4

Experimental method

X-RAY DIFFRACTION (1.76 Å)