1i2m
From Proteopedia
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|PDB= 1i2m |SIZE=350|CAPTION= <scene name='initialview01'>1i2m</scene>, resolution 1.76Å | |PDB= 1i2m |SIZE=350|CAPTION= <scene name='initialview01'>1i2m</scene>, resolution 1.76Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1a12|1a12]], [[1byu|1BYU]], [[1rrp|1RRP]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i2m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i2m OCA], [http://www.ebi.ac.uk/pdbsum/1i2m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i2m RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
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. | 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. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: Alveolar soft-part sarcoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606236 606236]], Osteolysis, familial expansile OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=603499 603499]], Paget disease of bone OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=603499 603499]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Renault, L.]] | [[Category: Renault, L.]] | ||
[[Category: Wittinghofer, A.]] | [[Category: Wittinghofer, A.]] | ||
| - | [[Category: SO4]] | ||
[[Category: beta-propeller]] | [[Category: beta-propeller]] | ||
[[Category: g fold or gtpase fold]] | [[Category: g fold or gtpase fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:13:43 2008'' |
Revision as of 18:13, 30 March 2008
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| , resolution 1.76Å | |||||||
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| Ligands: | |||||||
| Related: | 1a12, 1BYU, 1RRP
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
RAN-RCC1-SO4 COMPLEX
Overview
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.
About this Structure
1I2M is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for guanine nucleotide exchange on Ran by the regulator of chromosome condensation (RCC1)., Renault L, Kuhlmann J, Henkel A, Wittinghofer A, Cell. 2001 Apr 20;105(2):245-55. PMID:11336674
Page seeded by OCA on Sun Mar 30 21:13:43 2008
