1RPR
THE STRUCTURE OF COLE1 ROP IN SOLUTION
Summary for 1RPR
| Entry DOI | 10.2210/pdb1rpr/pdb |
| Descriptor | ROP (1 entity in total) |
| Functional Keywords | transcription regulation |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 14474.08 |
| Authors | Eberle, W.,Pastore, A.,Klaus, W.,Sander, C.,Roesch, P. (deposition date: 1991-10-09, release date: 1994-01-31, Last modification date: 2024-05-22) |
| Primary citation | Eberle, W.,Pastore, A.,Sander, C.,Rosch, P. The structure of ColE1 rop in solution. J.Biomol.NMR, 1:71-82, 1991 Cited by PubMed Abstract: The structure of the ColE1 repressor of primer (rop) protein in solution was determined from the proton nuclear magnetic resonance data by a combined use of distance geometry and restrained molecular dynamics calculations. A set of structures was determined with low internal energy and virtually no violations of the experimental distance restraints. Rop forms homodimers: Two helical hairpins are arranged as an antiparallel four helix bundle with a left-handed rope-like twist of the helix axes and with left-handed bundle topology. The very compact packing of the side chains in the helix interfaces of the rop coiled-coil structure may well account for its high stability. Overall, the solution structure is highly similar to the recently determined X-ray structure (Banner, D.W., Kokkinidis, M. and Tsernoglou, D. (1987) J. Mol. Biol., 196, 657-675), although there are minor differences in regions where packing forces appear to influence the crystal structure. PubMed: 1841691DOI: 10.1007/BF01874570 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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