SOLUTION STRUCTURE OF THE SINGLE-STRANDED-DNA BINDING-PROTEIN OF THE FILAMENTOUS PSEUDOMONAS PHAGE PF3 - SIMILARITY TO OTHER PROTEINS BINDING TO SINGLE-STRANDED NUCLEIC-ACIDS
Rha. Folmer et al., SOLUTION STRUCTURE OF THE SINGLE-STRANDED-DNA BINDING-PROTEIN OF THE FILAMENTOUS PSEUDOMONAS PHAGE PF3 - SIMILARITY TO OTHER PROTEINS BINDING TO SINGLE-STRANDED NUCLEIC-ACIDS, EMBO journal, 14(17), 1995, pp. 4132-4142
The three-dimensional structure of the homodimeric single-stranded DNA
binding protein encoded by the filamentous Pseudomonas bacteriophage
Pf3 has been determined using heteronuclear multidimensional NMR techn
iques and restrained molecular dynamics, NMR experiments and structure
calculations have been performed on a mutant protein (Phe36-->His) th
at was successfully designed to reduce the tendency of the protein to
aggregate, The protein monomer is composed of a five-stranded antipara
llel beta-sheet from which two beta-hairpins and a large loop protrude
, The structure is compared with the single-stranded DNA binding prote
in encoded by the filamentous Escherichia coli phage Ff, a protein wit
h a similar biological function and DNA binding properties, yet quite
different amino acid sequence, and with the major cold shock protein o
f Escherichia coli, a single-stranded DNA binding protein with an enti
rely different sequence, biological function and binding characteristi
cs. The amino acid sequence of the latter is highly homologous to the
nucleic acid binding domain (i.e. the cold shock domain) of proteins b
elonging to the Y-box family, Despite their differences in amino acid
sequence and function, the folds of the three proteins are remarkably
similar, suggesting that this is a preferred folding pattern shared by
many single-stranded DNA binding proteins.