1yd3
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Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Thermotoga maritima: Point mutant Y43F bound to its catalytic divalent cation
OverviewOverview
Nucleotide excision repair is a highly conserved DNA repair mechanism, present in all kingdoms of life. The incision reaction is a critical step, for damage removal and is accomplished by the UvrC protein in eubacteria., No structural information is so far available for the 3' incision, reaction. Here we report the crystal structure of the N-terminal catalytic, domain of UvrC at 1.5 A resolution, which catalyzes the 3' incision, reaction and shares homology with the catalytic domain of the GIY-YIG, family of intron-encoded homing endonucleases. The structure reveals a, patch of highly conserved residues surrounding a catalytic magnesium-water, cluster, suggesting that the metal binding site is an essential feature of, UvrC and all GIY-YIG endonuclease domains. Structural and biochemical data, strongly suggest that the N-terminal endonuclease domain of UvrC utilizes, a novel one-metal mechanism to cleave the phosphodiester bond.
About this StructureAbout this Structure
1YD3 is a Single protein structure of sequence from Thermotoga maritima with MN and GOL as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structural insights into the first incision reaction during nucleotide excision repair., Truglio JJ, Rhau B, Croteau DL, Wang L, Skorvaga M, Karakas E, DellaVecchia MJ, Wang H, Van Houten B, Kisker C, EMBO J. 2005 Mar 9;24(5):885-94. Epub 2005 Feb 3. PMID:15692561
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