1e69
From Proteopedia
(New page: 200px<br /><applet load="1e69" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e69, resolution 3.1Å" /> '''SMC HEAD DOMAIN FROM ...) |
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| - | [[Image:1e69.gif|left|200px]]<br /><applet load="1e69" size=" | + | [[Image:1e69.gif|left|200px]]<br /><applet load="1e69" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1e69, resolution 3.1Å" /> | caption="1e69, resolution 3.1Å" /> | ||
'''SMC HEAD DOMAIN FROM THERMOTOGA MARITIMA'''<br /> | '''SMC HEAD DOMAIN FROM THERMOTOGA MARITIMA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | SMC (structural maintenance of chromosomes) proteins are large coiled-coil | + | SMC (structural maintenance of chromosomes) proteins are large coiled-coil proteins involved in chromosome condensation, sister chromatid cohesion, and DNA double-strand break processing. They share a conserved five-domain architecture with three globular domains separated by two long coiled-coil segments. The coiled-coil segments are antiparallel, bringing the N and C-terminal globular domains together. We have expressed a fusion protein of the N and C-terminal globular domains of Thermotoga maritima SMC in Escherichia coli by replacing the approximately 900 residue coiled-coil and hinge segment with a short peptide linker. The SMC head domain (SMChd) binds and condenses DNA in an ATP-dependent manner. Using selenomethionine-substituted protein and multiple anomalous dispersion phasing, we have solved the crystal structure of the SMChd to 3.1 A resolution. In the monoclinic crystal form, six SMChd molecules form two turns of a helix. The fold of SMChd is closely related to the ATP-binding cassette (ABC) ATPase family of proteins and Rad50, a member of the SMC family involved in DNA double-strand break repair. In SMChd, the ABC ATPase fold is formed by the N and C-terminal domains with the 900 residue coiled-coil and hinge segment inserted in the middle of the fold. The crystal structure of an SMChd confirms that the coiled-coil segments in SMC proteins are anti-parallel and shows how the N and C-terminal domains come together to form an ABC ATPase. Comparison to the structure of the MukB N-terminal domain demonstrates the close relationship between MukB and SMC proteins, and indicates a helix to strand conversion when N and C-terminal parts come together. |
==About this Structure== | ==About this Structure== | ||
| - | 1E69 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http:// | + | 1E69 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E69 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
| - | [[Category: Cordell, S | + | [[Category: Cordell, S C.]] |
| - | [[Category: Ent, F | + | [[Category: Ent, F Van Den.]] |
[[Category: Lowe, J.]] | [[Category: Lowe, J.]] | ||
[[Category: coiled coil]] | [[Category: coiled coil]] | ||
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[[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 12:24:16 2008'' |
Revision as of 10:24, 21 February 2008
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SMC HEAD DOMAIN FROM THERMOTOGA MARITIMA
Overview
SMC (structural maintenance of chromosomes) proteins are large coiled-coil proteins involved in chromosome condensation, sister chromatid cohesion, and DNA double-strand break processing. They share a conserved five-domain architecture with three globular domains separated by two long coiled-coil segments. The coiled-coil segments are antiparallel, bringing the N and C-terminal globular domains together. We have expressed a fusion protein of the N and C-terminal globular domains of Thermotoga maritima SMC in Escherichia coli by replacing the approximately 900 residue coiled-coil and hinge segment with a short peptide linker. The SMC head domain (SMChd) binds and condenses DNA in an ATP-dependent manner. Using selenomethionine-substituted protein and multiple anomalous dispersion phasing, we have solved the crystal structure of the SMChd to 3.1 A resolution. In the monoclinic crystal form, six SMChd molecules form two turns of a helix. The fold of SMChd is closely related to the ATP-binding cassette (ABC) ATPase family of proteins and Rad50, a member of the SMC family involved in DNA double-strand break repair. In SMChd, the ABC ATPase fold is formed by the N and C-terminal domains with the 900 residue coiled-coil and hinge segment inserted in the middle of the fold. The crystal structure of an SMChd confirms that the coiled-coil segments in SMC proteins are anti-parallel and shows how the N and C-terminal domains come together to form an ABC ATPase. Comparison to the structure of the MukB N-terminal domain demonstrates the close relationship between MukB and SMC proteins, and indicates a helix to strand conversion when N and C-terminal parts come together.
About this Structure
1E69 is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
Crystal structure of the SMC head domain: an ABC ATPase with 900 residues antiparallel coiled-coil inserted., Lowe J, Cordell SC, van den Ent F, J Mol Biol. 2001 Feb 9;306(1):25-35. PMID:11178891
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