1xp8
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(New page: 200px<br /><applet load="1xp8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xp8, resolution 2.50Å" /> '''"Deinococcus radiodu...)
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Revision as of 04:07, 21 November 2007
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"Deinococcus radiodurans RecA in complex with ATP-gamma-S"
Overview
The resistance of Deinococcus radiodurans (Dr) to extreme doses of, ionizing radiation depends on its highly efficient capacity to repair, dsDNA breaks. Dr RecA, the key protein in the repair of dsDNA breaks by, homologous recombination, promotes DNA strand-exchange by an unprecedented, inverse pathway, in which the presynaptic filament is formed on dsDNA, instead of ssDNA. In order to gain insight into the remarkable repair, capacity of Dr and the novel mechanistic features of its RecA protein, we, have determined its X-ray crystal structure in complex with ATPgammaS at, 2.5A resolution. Like RecA from Escherichia coli, Dr RecA crystallizes as, a helical filament that is closely related to its biologically relevant, form, but with a more compressed pitch of 67 A. Although the overall fold, of Dr RecA is similar to E.coli RecA, there is a large reorientation of, the C-terminal domain, which in E.coli RecA has a site for binding dsDNA., Compared to E.coli RecA, the inner surface along the central axis of the, Dr RecA filament has an increased positive electrostatic potential. Unique, amino acid residues in Dr RecA cluster around a flexible beta-hairpin that, has also been implicated in DNA binding.
About this Structure
1XP8 is a Single protein structure of sequence from Deinococcus radiodurans with SAP as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of RecA from Deinococcus radiodurans: insights into the structural basis of extreme radioresistance., Rajan R, Bell CE, J Mol Biol. 2004 Dec 3;344(4):951-63. PMID:15544805
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