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| ===GCN4 - Leucine Zipper=== | | ===GCN4 - Leucine Zipper=== |
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| A specific DNA complex of the 65-residue, N-terminal fragment of the yeast transcriptional activator, GAL4, has been analysed at 2.7 A resolution by X-ray crystallography. The protein binds as a dimer to a symmetrical 17-base-pair sequence. A small, <scene name='Tom_Sandbox/Cd_binding/1'>Zn(2+)-containing domain </scene>recognizes a conserved CCG triplet at each end of the site through direct contacts with the major groove. A short coiled-coil dimerization element imposes 2-fold symmetry. A segment of extended polypeptide chain links the metal-binding module to the dimerization element and specifies the length of the site. The relatively open structure of the complex would allow another protein to bind coordinately with GAL4.
| | Blah blah information about leucine zipper GCN4. |
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| {{STRUCTURE_1ysa| PDB=1ysa | SCENE= }} | | {{STRUCTURE_1ysa| PDB=1ysa | SCENE= }} |
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| ==About this Structure== | | ==About this Structure== |
| [[2zta]] is a 2 chain structure formed by | | [[2zta]] is composed of two identical 52 residue alpha helix chains that grouped together to form a dimer. The dimer binds through interlocking leucine amino acids in the C terminal ends, while pinching in on the major groove of DNA in the N terminal end. |
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| ==See Also== | | ==See Also== |
| *[[Hydrogen in macromolecular models]]
| | [[2zta]] |
| | [[1ysa]] |
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| ==Reference== | | ==Reference== |
| <ref group="xtra">PMID:1557122</ref><references group="xtra"/>
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| [[Category: Saccharomyces cerevisiae]]
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| [[Category: Carey, M.]]
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| [[Category: Harrison, S C.]]
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| [[Category: Marmorstein, R.]]
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| [[Category: Ptashne, M.]]
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| [[Category: Double helix]]
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| [[Category: Protein-dna complex]]
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| [[Category: Transcription/dna complex]]
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