X-ray scattering indicates that the leucine zipper is a coiled coil
- Univ. of Utah School of Medicine, Salt Lake City (United States)
- Whitehead Inst. for Biomedical Research, Cambridge, MA (United States) Massachusetts Inst. of Tech., Cambridge (United States)
- Univ. of Utah School of Medicine, Salt Lake City (United States) Univ. of Utah, Salt Lake City (United States)
Dimerization of the bZIP class of eukaryotic transcriptional control proteins requires a sequence motif called the leucine zipper. The authors have grown two distinct crystal forms of a 33-amino acid peptide corresponding to the leucine zipper of the yeast transcriptional activator GCN4. This peptide is known to form a dimer of parallel helices in solution. X-ray scattering from both crystal forms shows reflections that are diagnostic of coiled coils. The most notable reflections occur at {approximately}5.2{angstrom} resolution and correspond to the pitch of helices in coiled coils. There is no diffraction maximum near 5.4{angstrom}, the characteristic pitch of straight helices. The results provide direct evidence that the leucine zipper of GCN4 is a coiled coil.
- OSTI ID:
- 5047319
- Journal Information:
- Proceedings of the National Academy of Sciences of the United States of America; (United States), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (United States) Vol. 88:2; ISSN 0027-8424; ISSN PNASA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
59 BASIC BIOLOGICAL SCIENCES
AMINO ACIDS
CARBOXYLIC ACIDS
COHERENT SCATTERING
CRYSTALLIZATION
DIFFRACTION
KERATIN
LEUCINE
MOLECULAR STRUCTURE
NUCLEOPROTEINS
ORGANIC ACIDS
ORGANIC COMPOUNDS
PHASE TRANSFORMATIONS
PROTEINS
SCATTERING
SCLEROPROTEINS
TRANSCRIPTION
TRANSCRIPTION FACTORS
X-RAY DIFFRACTION