User:Ann Taylor/Sandbox 1

Evaluating scenes representing the same structure

This sandbox compiles several student-generated scenes that illustrate properties of the Gal4 repressor.

Dimer

The protein binds as a to a symmetrical 17-base-pair sequence.

The protein binds as a to a symmetrical 17-base-pair sequence.

The protein binds as a to a symmetrical 17-base-pair sequence.

Domains

There is a compact (residues 8-40), an (41-49), and an (50-64).

, : Zinc is responsible for maintaining the secondary structure.

Each subunit folds into three distinct modules: a compact, (residues 8-40), an (41-49), and an alpha-helical (50-64).

Each subunit fold into three distinct modules: a compact, (residues 8-40), an (41-49), and an element (50-64).

Metal binding

A small, Zn(2+)-containing domain recognizes a conserved CCG triplet at each end of the site through direct contacts with the major groove. The metal binding domain contains that coordinate to the metal as shown as cadmium.

The cadmium is coordinated to this domain via interactions with several .

The Metal Binding Domain binds the metal through the use of .

DNA/protein interaction

The Upstream activation sequence () for Gal 4.

Gal4 also contains an upstream activating sequence () adjacent to that of the promoter region. This sequence works much like an enhancer regions that are common in Eukaryotic genes.

with all of the base pairs within 5 angstroms of the protein highlighted illustrates that the protein interacts with both strands of the UAS.