Human nucleotide excision repair protein xpa: summary of exafs studies on the zn (ii), co (ii) and cd (ii) associated minimal dna-binding domain

Title:Human nucleotide excision repair protein xpa: summary of exafs studies on the zn (ii), co (ii) and cd (ii) associated minimal dna-binding domain

Volume: 7 Issue: 1

Author(s): Garry W. Buchko, Nancy J. Hess and Michael A. Kennedy*

Affiliation:

• Pacific Northwest National Laboratories, Environmental Molecular Sciences Laboratory and Biogeochemistry Resources, Richland, WA 99352

Abstract: The zinc in the metal-binding core of the DNA-binding domain of the nucleotide excision repair protein XPA (M98-F219) can be replaced with cadmium (II) and cobalt (II). Here, we summarize extended X­ ray fine structure spectra collected on each protein in the lyophilized state and in 15% frozen aqueous glycerol solution. Under both conditions the Zn2•, Cd2+,and Co2• are tetrahedrally coordinated to the sulfur atom of four cysteine residues with the Zn-S and Co-S bond lengths nearly identical, at 2.34 A, and the Cd-S bond length at 2.54A.

Cite this article as:

Buchko W. Garry, Hess J. Nancy and Kennedy A. Michael*, Human nucleotide excision repair protein xpa: summary of exafs studies on the zn (ii), co (ii) and cd (ii) associated minimal dna-binding domain, Protein & Peptide Letters 2000; 7 (1) . https://dx.doi.org/10.2174/092986650701221205155907