MG_073_206_421_TETRAMER – DNA incision complex
Name | ||
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WID | MG_073_206_421_TETRAMER |
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Name | DNA incision complex |
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Cross references | PDB: 1QOJ | |
Structure | ||
Biosynthesis | [c]: MG_073_MONOMER + MG_206_MONOMER + (2) MG_421_MONOMER ⇒ MG_073_206_421_TETRAMER |
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No. subunits | 4 | |
DNA footprint | Length: 18 (nt), Binding: dsDNA, Region: dsDNA |
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Empirical formula (pH 7.5) | H25834C16022N4327O4717S76 | |
Molecular weight (pH 7.5; Da) | 356986.62 |
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Extinction coefficient (260 nm, 25C, pH 7.0) |
-242015.00 | |
Half life (OD (600 nm) = 0.3, M9 media, 36C; min) |
1200.00 |
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Synthesis | ||
Formation process | Process_MacromolecularComplexation |
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Localization | c | |
Function | ||
Enzyme | DNA incision [c]: ATP + (2) dRibose5P_dRibose5P + (3) H2O ⇒ ADP + (4) DR5P + (3) H + PI |
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Reaction participant |
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Complex subunit | DNA incision complex [c]: MG_073_MONOMER + MG_206_MONOMER + (2) MG_421_MONOMER ⇒ MG_073_206_421_TETRAMER |
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Parameters | ||
Parameters |
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Comments | ||
Comments | UvrA, UvrB, and UvrC form complexes that recognize DNA damage, and incise DNA 3' and 5' to damaged lesions in nucleotide excision repair. UvrA-C function according to the scheme below [PUB_0461]: UvrA2B complex recognizes DNA damage UvrA hydrolyzes ATP and dissociates from UvrB, leaving a DNA-UvrB complex UvrC complexes with UvrB, inducing a conformational change in UvrB which nicks the DNA 4 nt 3' to the damage UvrC nicks the DNA 7 nt 5' to the damage DNA-binding Distances between 3' and 5' cleavages is 12 bp [PUB_0461]. UvrAB footprint is 10 nt [PUB_0713], 18 nt [PUB_0709], 19 nt [PUB_0710], 20 nt [PUB_0712]. UvrA2 and UvrB have footprints of 33 nt and 24 nt [PUB_0515]. Composition [PUB_0006]. | |
References |
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Metadata | ||
Created | 2012-10-01 15:07:37 | |
Last updated | 2012-10-01 15:14:04 |