1qp9
From Proteopedia
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- | [[Image:1qp9.gif|left|200px]] | + | [[Image:1qp9.gif|left|200px]] |
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- | '''STRUCTURE OF HAP1-PC7 COMPLEXED TO THE UAS OF CYC7''' | + | {{Structure |
+ | |PDB= 1qp9 |SIZE=350|CAPTION= <scene name='initialview01'>1qp9</scene>, resolution 2.8Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''STRUCTURE OF HAP1-PC7 COMPLEXED TO THE UAS OF CYC7''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1QP9 is a [ | + | 1QP9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QP9 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11024163 11024163] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zinc binuclear cluster]] | [[Category: zinc binuclear cluster]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:40:47 2008'' |
Revision as of 11:40, 20 March 2008
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Coordinates: | save as pdb, mmCIF, xml |
STRUCTURE OF HAP1-PC7 COMPLEXED TO THE UAS OF CYC7
Overview
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.
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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