1wrs

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NMR STUDY OF HOLO TRP REPRESSOR

Overview

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.

About this Structure

1WRS is a Single protein structure of sequence from Escherichia coli with TRP as ligand. Full crystallographic information is available from OCA.

Reference

Refined solution structures of the Escherichia coli trp holo- and aporepressor., Zhao D, Arrowsmith CH, Jia X, Jardetzky O, J Mol Biol. 1993 Feb 5;229(3):735-46. PMID:8433368

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