1qp9
From Proteopedia
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|PDB= 1qp9 |SIZE=350|CAPTION= <scene name='initialview01'>1qp9</scene>, resolution 2.8Å | |PDB= 1qp9 |SIZE=350|CAPTION= <scene name='initialview01'>1qp9</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Lukens, A.]] | [[Category: Lukens, A.]] | ||
[[Category: Marmorstein, R.]] | [[Category: Marmorstein, R.]] | ||
| - | [[Category: ZN]] | ||
[[Category: coiled-coil]] | [[Category: coiled-coil]] | ||
[[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 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:17:01 2008'' |
Revision as of 20:17, 30 March 2008
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| , resolution 2.8Å | |||||||
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| Ligands: | , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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