1HBW

Solution nmr structure of the dimerization domain of the yeast transcriptional activator Gal4 (residues 50-106)

Summary for 1HBW

• Entry DOI: 10.2210/pdb1hbw/pdb
• Related: 1AW6 1D66
• NMR Information: BMRB: 5180
• Descriptor: REGULATORY PROTEIN GAL4 (1 entity in total)
• Functional Keywords: transcriptional activator, galactose and melibiose metabolism, dimerization domain, coiled-coil dimeric
• Biological source: SACCHAROMYCES CEREVISIAE (YEAST)
• Total number of polymer chains: 2
• Total formula weight: 13387.40

Authors

Hidalgo, P.,Ansari, A.Z.,Schmidt, P.,Hare, B.,Simkovic, N.,Farrell, S.,Shin, E.J.,Ptashne, M.,Wagner, G. (deposition date: 2001-04-20, release date: 2001-05-10, Last modification date: 2024-06-19)

Primary citation

Hidalgo, P.,Ansari, A.Z.,Schmidt, P.,Hare, B.,Simkovich, N.,Farrell, S.,Shin, E.J.,Ptashne, M.,Wagner, G.
Recruitment of the Transcriptional Machinery Through Gal11P: Structure and Interactions of the GAL4 Dimerization Domain
Genes Dev., 15:1007-, 2001

PubMed Abstract: The GAL4 dimerization domain (GAL4-dd) is a powerful transcriptional activator when tethered to DNA in a cell bearing a mutant of the GAL11 protein, named GAL11P. GAL11P (like GAL11) is a component of the RNA-polymerase II holoenzyme. Nuclear magnetic resonance (NMR) studies of GAL4-dd revealed an elongated dimer structure with C(2) symmetry containing three helices that mediate dimerization via coiled-coil contacts. The two loops between the three coiled coils form mobile bulges causing a variation of twist angles between the helix pairs. Chemical shift perturbation analysis mapped the GAL11P-binding site to the C-terminal helix alpha3 and the loop between alpha1 and alpha2. One GAL11P monomer binds to one GAL4-dd dimer rendering the dimer asymmetric and implying an extreme negative cooperativity mechanism. Alanine-scanning mutagenesis of GAL4-dd showed that the NMR-derived GAL11P-binding face is crucial for the novel transcriptional activating function of the GAL4-dd on GAL11P interaction. The binding of GAL4 to GAL11P, although an artificial interaction, represents a unique structural motif for an activating region capable of binding to a single target to effect gene expression.

PubMed: 11316794
DOI: 10.1101/GAD.873901

Experimental method

SOLUTION NMR