1xex
From Proteopedia
(New page: 200px<br /><applet load="1xex" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xex, resolution 2.5Å" /> '''Structural biochemist...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1xex.jpg|left|200px]]<br /><applet load="1xex" size=" | + | [[Image:1xex.jpg|left|200px]]<br /><applet load="1xex" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xex, resolution 2.5Å" /> | caption="1xex, resolution 2.5Å" /> | ||
'''Structural biochemistry of ATP-driven dimerization and DNA stimulated activation of SMC ATPases.'''<br /> | '''Structural biochemistry of ATP-driven dimerization and DNA stimulated activation of SMC ATPases.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Structural maintenance of chromosome (SMC) proteins play a central role in | + | 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== | ==About this Structure== | ||
| - | 1XEX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] with MG and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1XEX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XEX OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Pyrococcus furiosus]] | [[Category: Pyrococcus furiosus]] | ||
| - | [[Category: Hopfner, K | + | [[Category: Hopfner, K P.]] |
[[Category: Lammens, A.]] | [[Category: Lammens, A.]] | ||
[[Category: Schele, A.]] | [[Category: Schele, A.]] | ||
| Line 24: | Line 24: | ||
[[Category: structural maintenance of chromosomes]] | [[Category: structural maintenance of chromosomes]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:54:05 2008'' |
Revision as of 13:54, 21 February 2008
|
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 with and as ligands. 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
Page seeded by OCA on Thu Feb 21 15:54:05 2008
