1xex
From Proteopedia
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|PDB= 1xex |SIZE=350|CAPTION= <scene name='initialview01'>1xex</scene>, resolution 2.5Å | |PDB= 1xex |SIZE=350|CAPTION= <scene name='initialview01'>1xex</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= SMC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 Pyrococcus furiosus]) | |GENE= SMC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 Pyrococcus furiosus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1xew|1XEW]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xex OCA], [http://www.ebi.ac.uk/pdbsum/1xex PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xex RCSB]</span> | ||
}} | }} | ||
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[[Category: Lammens, A.]] | [[Category: Lammens, A.]] | ||
[[Category: Schele, A.]] | [[Category: Schele, A.]] | ||
| - | [[Category: ATP]] | ||
| - | [[Category: MG]] | ||
[[Category: abc-atpase]] | [[Category: abc-atpase]] | ||
[[Category: cohesin]] | [[Category: cohesin]] | ||
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[[Category: structural maintenance of chromosome]] | [[Category: structural maintenance of chromosome]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:48:40 2008'' |
Revision as of 21:48, 30 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | SMC (Pyrococcus furiosus) | ||||||
| Related: | 1XEW
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structural biochemistry of ATP-driven dimerization and DNA stimulated activation of SMC ATPases.
Overview
Structural maintenance of chromosome (SMC) proteins play a central role in higher-order chromosome structure in all kingdoms of life. SMC proteins consist of a long coiled-coil domain that joins an ATP binding cassette (ABC) ATPase domain on one side and a dimerization domain on the other side. SMC proteins require ATP binding or hydrolysis to promote cohesion and condensation, which is suggested to proceed via formation of SMC rings or assemblies. To learn more about the role of ATP in the architecture of SMC proteins, we report crystal structures of nucleotide-free and ATP bound P. furiosus SMC ATPase domains. ATP dimerizes two SMC ATPase domains by binding to opposing Walker A and signature motifs, indicating that ATP binding can directly assemble SMC proteins. DNA stimulates ATP hydrolysis in the engaged SMC ABC domains, suggesting that ATP hydrolysis can be allosterically regulated. Structural and mutagenesis data identify an SMC protein conserved-arginine finger that is required for DNA stimulation of the ATPase activity and directly connects a putative DNA interaction site to ATP. Our results suggest that stimulation of the SMC ATPase activity may be a specific feature to regulate the ATP-driven assembly and disassembly of SMC proteins.
About this Structure
1XEX is a Protein complex structure of sequences from Pyrococcus furiosus. Full crystallographic information is available from OCA.
Reference
Structural biochemistry of ATP-driven dimerization and DNA-stimulated activation of SMC ATPases., Lammens A, Schele A, Hopfner KP, Curr Biol. 2004 Oct 5;14(19):1778-82. PMID:15458651
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