Article
Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis.
Proteins - 1 Mar 1998
Schindler T, Perl D, Graumann P, Sieber V, Marahiel M A, Schmid F X
Abstract excerpt
In the cold-shock protein CspB from Bacillus subtilis three exposed Phe residues (F15, F17, and F27) are essential for its function in binding to single-stranded nucleic acids. Usually, the hydrophobic Phe side chains are buried in folded proteins. We asked here whether the exposition of the esse...
Topics
- Bacillus subtilis
- Bacterial Proteins
- Carrier Proteins
- Heat-Shock Proteins
- Mutation
- Nucleic Acids
- Phenylalanine
- Protein Binding
- Protein Conformation
- RNA-Binding Proteins
- Ribonucleoproteins
- Ribosomal Proteins