1e69
From Proteopedia
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| - | [[Image:1e69.gif|left|200px]] | + | [[Image:1e69.gif|left|200px]] |
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| - | '''SMC HEAD DOMAIN FROM THERMOTOGA MARITIMA''' | + | {{Structure |
| + | |PDB= 1e69 |SIZE=350|CAPTION= <scene name='initialview01'>1e69</scene>, resolution 3.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''SMC HEAD DOMAIN FROM THERMOTOGA MARITIMA''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1E69 is a [ | + | 1E69 is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11178891 11178891] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
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[[Category: coiled coil]] | [[Category: coiled coil]] | ||
[[Category: smc]] | [[Category: smc]] | ||
| - | [[Category: structural maintenance of | + | [[Category: structural maintenance of chromosome]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:50:28 2008'' |
Revision as of 08:50, 20 March 2008
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| , resolution 3.1Å | |||||||
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| 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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