PMID:9192620
| Citation |
Raghunathan, S, Ricard, CS, Lohman, TM and Waksman, G (1997) Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength x-ray diffraction on the selenomethionyl protein at 2.9-A resolution. Proc. Natl. Acad. Sci. U.S.A. 94:6652-7 |
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| Abstract |
The crystal structure of the tetrameric DNA-binding domain of the single-stranded DNA binding protein from Escherichia coli was determined at a resolution of 2.9 A using multiwavelength anomalous dispersion. Each monomer in the tetramer is topologically similar to an oligomer-binding fold. Two monomers each contribute three beta-strands to a single six-stranded beta-sheet to form a dimer. Two dimer-dimer interfaces are observed within the crystal. One of these stabilizes the tetramer in solution. The other interface promotes a superhelical structure within the crystal that may reflect tetramer-tetramer interactions involved in the positive cooperative binding of the single-stranded DNA-binding protein to single-stranded DNA. |
| Links | |
| Keywords |
Amino Acid Sequence; Binding Sites; Crystallography, X-Ray; DNA, Single-Stranded/metabolism; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/metabolism; Escherichia coli/chemistry; Models, Molecular; Molecular Sequence Data; Protein Conformation |
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