Format

Send to

Choose Destination
Nat Commun. 2015 Jun 15;6:7283. doi: 10.1038/ncomms8283.

A network of molecular switches controls the activation of the two-component response regulator NtrC.

Author information

1
Department of Chemistry, Stanford University, Stanford, California 94305, USA.
2
1] Department of Chemistry, Stanford University, Stanford, California 94305, USA [2] SIMBIOS NIH Center for Biomedical Computation, Stanford University, Stanford, California 94305,USA [3] Department of Chemical and Bimolecular Engineering, University of Illinois at Urbana-Champaign, Urbana, Illionios 61801, USA.
3
1] Department of Chemistry, Stanford University, Stanford, California 94305, USA [2] SIMBIOS NIH Center for Biomedical Computation, Stanford University, Stanford, California 94305,USA.

Abstract

Recent successes in simulating protein structure and folding dynamics have demonstrated the power of molecular dynamics to predict the long timescale behaviour of proteins. Here, we extend and improve these methods to predict molecular switches that characterize conformational change pathways between the active and inactive state of nitrogen regulatory protein C (NtrC). By employing unbiased Markov state model-based molecular dynamics simulations, we construct a dynamic picture of the activation pathways of this key bacterial signalling protein that is consistent with experimental observations and predicts new mutants that could be used for validation of the mechanism. Moreover, these results suggest a novel mechanistic paradigm for conformational switching.

PMID:
26073186
DOI:
10.1038/ncomms8283
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Nature Publishing Group
Loading ...
Support Center