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Structure and inherent properties of the bacteriophage lambda head shell
- Source :
- Journal of Molecular Biology. 213:503-511
- Publication Year :
- 1990
- Publisher :
- Elsevier BV, 1990.
-
Abstract
- Some mutations in the major capsid protein (gpE) of λ phage can alter the size and shape of the head shell or block the pathway of head maturation. Previous studies on the classification of such mutants showed that there are at least five functional sites on the gpE molecule. In this study, we determined the amino acid exchanges by DNA sequencing to elucidate the molecular design of the form-determining multifunctional protein gpE. In addition, we characterized the mutated gpE molecules by two-dimensional gel electrophoresis and studied suppression patterns of amber mutants at 43 amino acid residues. Those mutations map at 19 amino acid residues at 22 bases, which are located in three regions, 40 to 91, 222 to 246, and 284 to 324 of the 341 amino acid residues of gpE. These regions seem to be important in the activity of gpE, since amber mutations in these regions are suppressed on the average by less species of suppressors than those outside these regions. The mutations having different phenotypes are not segregated from each other, while some mutations having the same phenotype are separated far apart in the primary structure. This suggests that the functional sites were formed during evolution after the folding pattern of the ancestral gpE polypeptide chain had been established. Many of the mutations are located at serine, glycine and proline residues in predicted β -turns.
- Subjects :
- chemistry.chemical_classification
Gel electrophoresis
Circular dichroism
Conformational change
Absorption spectroscopy
biology
Chemistry
Intermolecular force
Mutant
Protein primary structure
Prohead
Tetranitromethane
biology.organism_classification
Amino acid
Serine
Bacteriophage
Crystallography
chemistry.chemical_compound
Biochemistry
Capsid
Structural Biology
Glycine
Molecule
Protein secondary structure
Molecular Biology
Subjects
Details
- ISSN :
- 00222836
- Volume :
- 213
- Database :
- OpenAIRE
- Journal :
- Journal of Molecular Biology
- Accession number :
- edsair.doi.dedup.....1cf0bcbae9607e5b84deb664127e2f11