 |
PDBsum entry 1d66
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Transcription/DNA
|
PDB id
|
|
|
|
1d66
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Dna recognition by gal4: structure of a protein-Dna complex.
|
|
|
Authors
|
|
R.Marmorstein,
M.Carey,
M.Ptashne,
S.C.Harrison.
|
|
|
Ref.
|
|
Nature, 1992,
356,
408-414.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
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, 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.
|
|
|
|
|
|
|
