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- | [[Image:1qp9.gif|left|200px]] | + | {{Seed}} |
| + | [[Image:1qp9.png|left|200px]] |
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| {{STRUCTURE_1qp9| PDB=1qp9 | SCENE= }} | | {{STRUCTURE_1qp9| PDB=1qp9 | SCENE= }} |
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- | '''STRUCTURE OF HAP1-PC7 COMPLEXED TO THE UAS OF CYC7'''
| + | ===STRUCTURE OF HAP1-PC7 COMPLEXED TO THE UAS OF CYC7=== |
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- | ==Overview==
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- | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11024163}}, adds the Publication Abstract to the page |
| + | (as it appears on PubMed at http://www.pubmed.gov), where 11024163 is the PubMed ID number. |
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| + | {{ABSTRACT_PUBMED_11024163}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Heptad repeat]] | | [[Category: Heptad repeat]] |
| [[Category: Zinc binuclear cluster]] | | [[Category: Zinc binuclear cluster]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:32:43 2008'' | + | |
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:49:53 2008'' |
Revision as of 02:49, 28 July 2008
Template:STRUCTURE 1qp9
STRUCTURE OF HAP1-PC7 COMPLEXED TO THE UAS OF CYC7
Template:ABSTRACT PUBMED 11024163
About this Structure
1QP9 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structure of HAP1-PC7 bound to DNA: implications for DNA recognition and allosteric effects of DNA-binding on transcriptional activation., Lukens AK, King DA, Marmorstein R, Nucleic Acids Res. 2000 Oct 15;28(20):3853-63. PMID:11024163
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