1QP9

STRUCTURE OF HAP1-PC7 COMPLEXED TO THE UAS OF CYC7

Summary for 1QP9

• Entry DOI: 10.2210/pdb1qp9/pdb
• Descriptor: DNA (5'-D(*AP*CP*GP*CP*TP*AP*TP*TP*AP*TP*CP*GP*CP*TP*AP*TP*TP*AP*GP*T)-3'), DNA (5'-D(*AP*CP*TP*AP*AP*TP*AP*GP*CP*GP*AP*TP*AP*AP*TP*AP*GP*CP*GP*T)-3'), CYP1(HAP1-PC7) ACTIVATORY PROTEIN, ... (5 entities in total)
• Functional Keywords: zinc binuclear cluster, coiled-coil, heptad repeat, transcription-dna complex, transcription/dna
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Total number of polymer chains: 8
• Total formula weight: 61469.98

Authors

Lukens, A.,King, D.,Marmorstein, R. (deposition date: 1999-06-01, release date: 2000-10-09, Last modification date: 2024-02-14)

Primary citation

Lukens, A.K.,King, D.A.,Marmorstein, R.
Structure of HAP1-PC7 bound to DNA: implications for DNA recognition and allosteric effects of DNA-binding on transcriptional activation.
Nucleic Acids Res., 28:3853-3863, 2000

PubMed Abstract: HAP1 is a transcription factor in yeast whose DNA-binding domain has been implicated in directly affecting transcriptional activation. Two separate mutations in the DNA-binding domain, S63G (HAP1-PC7) and S63R (HAP1-18), retain wild-type binding affinity. However, HAP1-PC7 is transcriptionally silent while HAP1-18 shows highly elevated levels of transcription. We have determined the X-ray crystal structure of the DNA-binding domain of HAP1-PC7 bound to its DNA target, UAS(CYC7), and compared it to the previously solved HAP1-wt and HAP1-18 complexes to UAS(CYC7). Additionally, we have quantitatively compared the DNA-binding affinity and specificity of the HAP1-PC7, HAP1-18 and HAP1-wt DNA-binding domains. We show that, although the DNA-binding domains of these three proteins bind UAS(CYC7) with comparable affinity and specificity, the protein-DNA interactions are dramatically different between the three complexes. Conserved protein-DNA interactions are largely restricted to an internal DNA sequence that excludes one of the two conserved DNA half-sites of UAS(CYC7) suggesting a mode of recognition distinct from other HAP1 family members. Alternative protein-DNA interactions result in divergent DNA configurations between the three complexes. These results suggest that the differential transcriptional activities of the HAP1, HAP1-18 and HAP1-PC7 proteins are due, at least in part, to alternative protein-DNA contacts, and implies that HAP1-DNA interactions have direct allosteric effects on transcriptional activation.

PubMed: 11024163
DOI: 10.1093/nar/28.20.3853

Experimental method

X-RAY DIFFRACTION (2.8 Å)