Taylor Gal4 Sandbox

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1d66, resolution 2.70Å (default scene)
Ligands:	CD
Structural annotation: Resources: CATH : 1D66B01 InterPro : Ipr007219, Ipr005600, Ipr001138, Ipr002409 Pfam : PF00172, PF03902 SCOP : d1d66a2, d1d66a1, d1d66b1, d1d66b2 UniProt : P04386
Functional annotation: Cellular component: nucleus Biological process: carbohydrate metabolic process positive regulation of transcription by galactose transcription galactose metabolic process regulation of transcription, DNA-dependent Molecular function: transcription factor activity DNA binding metal ion binding transcription activator activity zinc ion binding
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

DNA RECOGNITION BY GAL4: STRUCTURE OF A PROTEIN/DNA COMPLEX

GAL4 is a transcription factor that induces genes required for the metabolism of galactose, specifically enzymes involved in the conversion of galactose to glucose. This structure is for the DNA binding domain of GAL4, and contains 65 residues from the N terminus. The protein binds as a dimer to a symmetrical 17-base-pair sequence. Each subunit folds into three distinct modules: a compact, metal binding domain(residues 8-40), an extended linker(41-49), and an alpha-helical dimerization element (50-64). The small, Zn(2+)-containing domain, which contains two metal ions tetrahedrally coordinated by six cysteines. This metal binding 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.

About this Structure

1d66 is a 4 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

See Also

• Hydrogen in macromolecular models

Proteopedia Page Contributors and Editors (what is this?)

Ann Taylor