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"Evidence from extended X-ray absorption fine structure and site-specific mutagenesis for zinc fingers in UvrA protein of Escherichia coli." |
Navaratnam S, Myles GM, Strange RW, Sancar A |
Published Sept. 25, 1989 in J Biol Chem volume 264 .
Pubmed ID: 2550431
Abstract:
| The UvrA protein is the damage recognition subunit of the Escherichia coli repair enzyme ABC excision nuclease. Sequence analysis of this 940-amino acid protein revealed two regions of sequence homology to the zinc finger motif found in many DNA binding proteins. Physical and chemical analyses indicate about 2 zinc atoms/molecule. We have used extended x-ray absorption fine structure analysis to demonstrate that each of these zinc atoms is coordinated with 4 cysteine residues at a distance of 2.32 +/- 0.2 A. Substitution of one of the cysteines by a histidine, a serine, or an alanine in one of the potential finger sites resulted in a respective decrease in complementing activity. We thus conclude that the two zinc fingers identified by sequence analysis do indeed have zinc finger structure in UvrA protein. |
This publication refers to following REPAIRtoire entries:
| Genes | |
| Proteins |
Last modification of this entry: Oct. 6, 2010
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