Zinc co-ordination in the DNA-binding domain of the yeast transcriptional activator PPR1.
The structure of the native zinc form of the DNA binding domain in the yeast transcriptional activator PPR1 was investigated by extended X-ray absorption fine structure (EXAFS). By carrying out the EXAFS measurements at 11k we were able to demonstrate explicitly the proximity of the two zinc ions (Zn-Zn distance = 3.16 +/- 0.03 A) and the presence of bridging cysteine ligands. The results show that the six cysteine residues co-ordinate two zinc ions in a two-metal ion cluster. PPR1 is the first member of this class of protein for which such information has been obtained.
Ball
L J
LJ
DRAL, Daresbury Laboratory, Warrington, UK.
Diakun
G P
GP
Gadhavi
P L
PL
Young
N A
NA
Armstrong
E M
EM
Garner
C D
CD
Laue
E D
ED
D001665:Binding Sites; D004268:DNA-Binding Proteins / Q000737:chemistry*; D005656:Fungal Proteins / Q000737:chemistry*; D029701:Saccharomyces cerevisiae Proteins; D013052:Spectrometry, X-Ray Emission; D014157:Transcription Factors / Q000737:chemistry*; D015032:Zinc / Q000737:chemistry*
D004268:DNA-Binding Proteins; D005656:Fungal Proteins; C065682:PPR1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D015032:Zinc