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2hap
From Proteopedia
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|PDB= 2hap |SIZE=350|CAPTION= <scene name='initialview01'>2hap</scene>, resolution 2.5Å | |PDB= 2hap |SIZE=350|CAPTION= <scene name='initialview01'>2hap</scene>, resolution 2.5Å | ||
|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=2hap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hap OCA], [http://www.ebi.ac.uk/pdbsum/2hap PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hap RCSB]</span> | ||
}} | }} | ||
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[[Category: Marmorstein, R.]] | [[Category: Marmorstein, R.]] | ||
[[Category: Zhang, L.]] | [[Category: Zhang, L.]] | ||
| - | [[Category: ZN]] | ||
[[Category: asymmetry]] | [[Category: asymmetry]] | ||
[[Category: complex transcription factor/dna]] | [[Category: complex transcription factor/dna]] | ||
| Line 32: | Line 34: | ||
[[Category: transcriptional activation]] | [[Category: transcriptional activation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:27:48 2008'' |
Revision as of 00:27, 31 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF A HAP1-18/DNA COMPLEX REVEALS THAT PROTEIN/DNA INTERACTIONS CAN HAVE DIRECT ALLOSTERIC EFFECTS ON TRANSCRIPTIONAL ACTIVATION
Overview
HAP1 is a yeast transcriptional activator that binds with equal affinity to the dissimilar upstream activation sequences UAS1 and UAS(CYC7), but activates transcription differentially when bound to each site. HAP1-18 harbors an amino acid change in the DNA binding domain. While binding UAS1 poorly, HAP1-18 binds UAS(CYC7) with wild-type properties and activates transcription at elevated levels relative to HAP1. We have determined the structure of HAP1-18-UAS(CYC7) and have compared it to HAP1-UAS(CYC7). Unexpectedly, the single amino acid substitution in HAP1-18 nucleates a significantly altered hydrogen bond interface between the protein and DNA resulting in DNA conformational changes and an ordering of one N-terminal arm of the protein dimer along the DNA minor groove. These observations, together with a large subset of transcriptionally defective mutations in the HAP1 DNA-binding domain that map to the HAP1-DNA interface, suggest that protein-DNA interactions may have direct allosteric effects on transcriptional activation.
About this Structure
2HAP is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structure of HAP1-18-DNA implicates direct allosteric effect of protein-DNA interactions on transcriptional activation., King DA, Zhang L, Guarente L, Marmorstein R, Nat Struct Biol. 1999 Jan;6(1):22-7. PMID:9886287
Page seeded by OCA on Mon Mar 31 03:27:48 2008
