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PDBsum entry 1i2m
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structural basis for guanine nucleotide exchange on ran by the regulator of chromosome condensation (rcc1).
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Authors
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L.Renault,
J.Kuhlmann,
A.Henkel,
A.Wittinghofer.
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Ref.
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Cell, 2001,
105,
245-255.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 1.
Figure 1. Overall View of the Ran.RCC1 complex
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Figure 3.
Figure 3. Contact Residues in the Complex
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2001,
105,
245-255)
copyright 2001.
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