1e69
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e69 OCA], [http://www.ebi.ac.uk/pdbsum/1e69 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e69 RCSB]</span> | ||
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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 Sun Mar 30 19:56:04 2008'' |
Revision as of 16:56, 30 March 2008
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| , resolution 3.1Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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