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Refined solution structures of the Escherichia coli trp holo- and aporepressor.

Zhao D, Arrowsmith CH, Jia X, Jardetzky O
J Mol Biol 229 735-46 (1993)
Related entries: 1rcs, 1wrt

Cited: 55 times
EuropePMC logo PMID: 8433368

Abstract

The solution structures of the trp-repressor from Escherichia coli in both the liganded (holo-) and unliganded (apo-) form, have been refined by restrained molecular dynamics with simulated annealing using the program XPLOR and additional experimental constraints. The ensemble of refined holorepressor structures have a root-mean-square deviation (r.m.s.d.) of 0.8 A relative to the average structure for the backbone of the dimer core (helices A, B, C, A', B', C') and 2.5 A for the helix-turn-helix DNA-binding domain (helices D and E). The corresponding values for the aporepressor are 0.9 A for the backbone of the ABC-dimer core and 3.2 A for the DE helix-turn-helix. The r.m.s.d. of the average structures from the corresponding crystal structures are 2.3 A for the holorepressor ABC core and 4.2 A for its DE region; 2.3 A for the aporepressor core and 5.5 A for its DE region. The relative disorder of the DNA-binding domain is reflected in a number of experimental parameters including substantially more rapid backbone proton exchange rates, exchange-limited relaxation times and crystallographic B-factors. The stabilizing effect of the L-Trp ligand is evident in these measurements, as it is in the higher precision of the holorepressor structure.

Articles - 1wrs mentioned but not cited (1)

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Related citations provided by authors (5)

  1. The solution structures of the trp repressor-operator DNA complex.. Zhang H, Zhao D, Revington M, Lee W, Jia X, Arrowsmith C, Jardetzky O J Mol Biol 238 592-614 (1994)
  2. Sequential Simulated Annealing: An Efficient Procedure for Structural Refinement Based on NMR Constraints. Zhao D, Jardetzky O J Phys Chem 97 3007- (1993)
  3. The solution structures of Escherichia coli trp repressor and trp aporepressor at an intermediate resolution.. Arrowsmith C, Pachter R, Altman R, Jardetzky O Eur J Biochem 202 53-66 (1991)
  4. Sequence-specific 1H NMR assignments and secondary structure in solution of Escherichia coli trp repressor.. Arrowsmith CH, Pachter R, Altman RB, Iyer SB, Jardetzky O Biochemistry 29 6332-41 (1990)
  5. NMR assignments for the amino-terminal residues of trp repressor and their role in DNA binding.. Arrowsmith CH, Carey J, Treat-Clemons L, Jardetzky O Biochemistry 28 3875-9 (1989)

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