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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| - | 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 <scene name='92/925551/Dimer_practice/1'>dimer</scene> to a symmetrical 17-base-pair sequence. Each subunit folds into three distinct modules: a compact, <scene name='92/925551/Dimer_practice/ | + | 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 <scene name='92/925551/Dimer_practice/1'>dimer</scene> to a symmetrical 17-base-pair sequence. Each subunit folds into three distinct modules: a compact, <scene name='92/925551/Dimer_practice/12'>Metal Binding Domain</scene> (residues 8-40), an <scene name='92/925551/Dimer_practice/4'>Extended Linker</scene> (41-49), and an alpha-helical <scene name='92/925551/Dimer_practice/7'>Dimerization Element</scene> (50-64). A small, Zn(2+)-containing domain 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. |
Gal4 <scene name='92/925551/Practice/1'>practice structure</scene> | Gal4 <scene name='92/925551/Practice/1'>practice structure</scene> | ||
Revision as of 02:55, 20 September 2022
DNA RECOGNITION BY GAL4: STRUCTURE OF A PROTEIN/DNA COMPLEX
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