Tom Sandbox: Difference between revisions
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[[Image: | [[Image:2zta.png|left|200px]] | ||
{{ | {{STRUCTURE_2zta| PDB=2zta | SCENE= }} | ||
===DNA RECOGNITION BY GAL4: STRUCTURE OF A PROTEIN/DNA COMPLEX=== | ===DNA RECOGNITION BY GAL4: STRUCTURE OF A PROTEIN/DNA COMPLEX=== | ||
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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. | 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. | ||
{{ | {{STRUCTURE_1ysa| PDB=1ysa | SCENE= }} | ||
==About this Structure== | ==About this Structure== | ||
