1pyc
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CYP1 (HAP1) DNA-BINDING DOMAIN (RESIDUES 60-100), NMR, 15 STRUCTURES
OverviewOverview
CYP1(HAP1) is a transcriptional activator involved in the aerobic, metabolism of the yeast Saccharomyces cerevisiae. The amino acid sequence, of its DNA-binding domain suggests that it belongs to the "zinc cluster", class. This region is indeed characterized by a pattern known to form a, bimetal thiolate cluster where two zinc ions are coordinated by six, cysteine residues. Structures of two such domains, those from GAL4 and, PPR1, have been solved as complexes with DNA. These domains consist of the, zinc cluster connected to a dimerization helix by a linker peptide. They, recognize, as a dimer, an inverted repeat of a CGG motif that is separated, by a specific number of bases. Interestingly, the specificity of that, interaction seems not to be due to the interaction between the cluster, region and the DNA but rather to a fine tune between the structure of the, linker peptide and the number of base-pairs separating the two CGGs., However, the CYP1 target sites fail to display such a consensus sequence., One of the two CGG sites is poorly conserved and some experiments suggest, a direct rather than an inverted repeat. Using 1H, 15N and 113Cd NMR, spectroscopy, we have undertaken the analysis of the structural properties, of the CYP1(56-126) fragment that consists of the zinc-cluster region, the, linker peptide and a part of the dimerization helix. We have demonstrated, that the six cysteine residues of the peptide chelate two cadmium ions as, in GAL4 and PPR1. Fifteen structures of the zinc-cluster region (residues, 60 to 100) were calculated, the linker peptide and the dimerization helix, being unstructured under the conditions of our study. This region, possesses the same overall fold as in GAL4 and PPR1, and most of the, side-chains involved in the interaction with DNA are structurally, conserved. This suggests that the CYP1 zinc-cluster region recognizes a, CGG triplet in the same way as GAL4 and PPR1. In this case, the particular, properties of CYP1 seem to be due to the structure of the linker peptide, and/or of the dimerization helix.
About this StructureAbout this Structure
1PYC is a Single protein structure of sequence from Saccharomyces cerevisiae with ZN as ligand. Full crystallographic information is available from OCA.
ReferenceReference
1H, 15N resonance assignment and three-dimensional structure of CYP1 (HAP1) DNA-binding domain., Timmerman J, Vuidepot AL, Bontems F, Lallemand JY, Gervais M, Shechter E, Guiard B, J Mol Biol. 1996 Jun 21;259(4):792-804. PMID:8683583
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