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| - | [[Image:1e69.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1e69| PDB=1e69 | SCENE= }} | | {{STRUCTURE_1e69| PDB=1e69 | SCENE= }} |
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| - | '''SMC HEAD DOMAIN FROM THERMOTOGA MARITIMA'''
| + | ===SMC HEAD DOMAIN FROM THERMOTOGA MARITIMA=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11178891}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11178891 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11178891}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Smc]] | | [[Category: Smc]] |
| | [[Category: Structural maintenance of chromosome]] | | [[Category: Structural maintenance of chromosome]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:43:01 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:13:05 2008'' |
Revision as of 21:13, 30 June 2008
Template:STRUCTURE 1e69
SMC HEAD DOMAIN FROM THERMOTOGA MARITIMA
Template:ABSTRACT PUBMED 11178891
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
Page seeded by OCA on Tue Jul 1 00:13:05 2008
