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