1pfs
From Proteopedia
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SOLUTION NMR STRUCTURE OF THE SINGLE-STRANDED DNA BINDING PROTEIN OF THE FILAMENTOUS PSEUDOMONAS PHAGE PF3, MINIMIZED AVERAGE STRUCTURE
Overview
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 techniques, and restrained molecular dynamics. NMR experiments and structure, calculations have been performed on a mutant protein (Phe36 --> His) that, was successfully designed to reduce the tendency of the protein to, aggregate. The protein monomer is composed of a five-stranded antiparallel, beta-sheet from which two beta-hairpins and a large loop protrude. The, structure is compared with the single-stranded DNA binding protein encoded, by the filamentous Escherichia coli phage Ff, a protein with a similar, biological function and DNA binding properties, yet quite different amino, acid sequence, and with the major cold shock protein of Escherichia coli, a single-stranded DNA binding protein with an entirely different sequence, biological function and binding characteristics. The amino acid sequence, of the latter is highly homologous to the nucleic acid binding domain, (i.e. the cold shock domain) of proteins belonging 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.
About this Structure
1PFS is a Single protein structure of sequence from Pseudomonas phage pf3. Full crystallographic information is available from OCA.
Reference
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., Folmer RH, Nilges M, Konings RN, Hilbers CW, EMBO J. 1995 Sep 1;14(17):4132-42. PMID:7556054
Page seeded by OCA on Tue Nov 20 23:45:57 2007
