The structure of ColE1 rop in solution |
| |
Authors: | W Eberle A Pastore C Sander P Rösch |
| |
Institution: | (1) European Molecular Biology Laboratory, Meyerhofstr. 1, D-6900 Heidelberg 1, Germany;(2) Department of Biophysics, Max-Planck-Institute for Medical Research, Jahnstr. 29, D-6900 Heidelberg 1, Germany;(3) Department of Structure and Chemistry of Biopolymers, University of Bayreuth, P.O. Box 10 12 51, D-8580 Bayreuth, Germany |
| |
Abstract: | Summary 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.Abbreviations rop
repressor of primer
- NMR
nuclear magnetic resonance
- NOE
nuclear Overhauser enhancement
- NOESY
NOE spectroscopy
- RAN Set
Structures generated from random choice of the dihedrai angles
- HEL Set
Structures generated from random choice of the dihedral angles restricted to ranges allowed for helices
- MD
molecular dynamics
- EM
energy minimization
- RMSD
root-mean-square deviation of atomic positions |
| |
Keywords: | rop Protein conformation 2D NMR Molecular dynamics Repressor proteins |
本文献已被 SpringerLink 等数据库收录! |
|