An alternative flexible conformation of the E. coli HU beta(2) protein: structural, dynamics, and functional aspects

Abstract : The histone-like HU protein is the major nucleoid-associated protein involved in the dynamics and structure of the bacterial chromosome. Under physiological conditions, the three possible dimeric forms of the E. coli HU protein (EcHU alpha(2), EcHU beta(2), and EcHU alpha beta) are in thermal equilibrium between two dimeric conformations (N-2 a dagger" I-2) varying in their secondary structure content. High-temperature molecular dynamics simulations combined with NMR experiments provide information about structural and dynamics features at the atomic level for the N-2 to I-2 thermal transition of the EcHU beta(2) homodimer. On the basis of these data, a realistic 3D model is proposed for the major I-2 conformation of EcHU beta(2). This model is in agreement with previous experimental data.
Document type :
Journal articles
Complete list of metadatas

https://hal.archives-ouvertes.fr/hal-00602370
Contributor : Isabelle Frapart <>
Submitted on : Wednesday, June 22, 2011 - 11:03:14 AM
Last modification on : Tuesday, May 14, 2019 - 8:50:05 AM

Links full text

Identifiers

Collections

Citation

Norbert Garnier, Karine Loth, Franck Coste, Rafal Augustyniak, Virginie Nadan, et al.. An alternative flexible conformation of the E. coli HU beta(2) protein: structural, dynamics, and functional aspects. European Biophysics Journal, Springer Verlag (Germany), 2011, 40 (2), pp.117-129. ⟨10.1007/s00249-010-0630-y⟩. ⟨hal-00602370⟩

Share

Metrics

Record views

193