5TM0

Solution NMR structures of two alternative conformations of E. coli tryptophan repressor in dynamic equilibrium

Summary for 5TM0

• Entry DOI: 10.2210/pdb5tm0/pdb
• NMR Information: BMRB: 26821
• Descriptor: Trp operon repressor (1 entity in total)
• Functional Keywords: structural genomics, psi-biology, northeast structural genomics consortium, nesg, transcription
• Biological source: Escherichia coli O157:H7
• Cellular location: Cytoplasm : P0A882
• Total number of polymer chains: 4
• Total formula weight: 49480.52

Authors

Harish, B.,Swapna, G.V.T.,Kornhaber, G.J.,Montelione, G.T.,Carey, J.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2016-10-12, release date: 2017-10-25, Last modification date: 2024-05-15)

Primary citation

Harish, B.,Swapna, G.V.,Kornhaber, G.J.,Montelione, G.T.,Carey, J.
Multiple helical conformations of the helix-turn-helix region revealed by NOE-restrained MD simulations of tryptophan aporepressor, TrpR.
Proteins, 85:731-740, 2017

PubMed Abstract: The nature of flexibility in the helix-turn-helix region of E. coli trp aporepressor has been unexplained for many years. The original ensemble of nuclear magnetic resonance (NMR structures showed apparent disorder, but chemical shift and relaxation measurements indicated a helical region. Nuclear Overhauser effect (NOE) data for a temperature-sensitive mutant showed more helical character in its helix-turn-helix region, but nevertheless also led to an apparently disordered ensemble. However, conventional NMR structure determination methods require all structures in the ensemble to be consistent with every NOE simultaneously. This work uses an alternative approach in which some structures of the ensemble are allowed to violate some NOEs to permit modeling of multiple conformational states that are in dynamic equilibrium. Newly measured NOE data for wild-type aporepressor are used as time-averaged distance restraints in molecular dynamics simulations to generate an ensemble of helical conformations that is more consistent with the observed NMR data than the apparent disorder in the previously reported NMR structures. The results indicate the presence of alternating helical conformations that provide a better explanation for the flexibility of the helix-turn-helix region of trp aporepressor. Structures representing these conformations have been deposited with PDB ID: 5TM0. Proteins 2017; 85:731-740. © 2016 Wiley Periodicals, Inc.

PubMed: 28120439
DOI: 10.1002/prot.25252

Experimental method

SOLUTION NMR