1qp9

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[[Image:1qp9.gif|left|200px]]
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{{Structure
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{{STRUCTURE_1qp9| PDB=1qp9 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qp9 OCA], [http://www.ebi.ac.uk/pdbsum/1qp9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qp9 RCSB]</span>
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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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[[Category: Lukens, A.]]
[[Category: Lukens, A.]]
[[Category: Marmorstein, R.]]
[[Category: Marmorstein, R.]]
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[[Category: coiled-coil]]
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[[Category: Coiled-coil]]
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[[Category: heptad repeat]]
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[[Category: Heptad repeat]]
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[[Category: zinc binuclear cluster]]
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[[Category: Zinc binuclear cluster]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:32:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:17:01 2008''
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Revision as of 03:32, 3 May 2008

Template:STRUCTURE 1qp9

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 Page seeded by OCA on Sat May 3 06:32:43 2008

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