Ultrafast structural dynamics of BlsA, a photoreceptor from the pathogenic bacterium Acinetobacter baumannii

Richard Brust, Allison Haigney, Andras Lukacs, Agnieszka Gil, Shahrier Hossain, Kiri Addison, Cheng-Tsung Lai, Michael Towrie, Gregory M. Greetham, Ian P. Clark, Boris Illarionov, Adelbert Bacher, Ryu-Ryun Kim, Markus Fischer, Carlos Simmerling, Stephen R. Meech, Peter J. Tonge

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Acinetobacter baumannii is an important human pathogen that can form biofilms and persist under harsh environmental conditions. Biofilm formation and virulence are modulated by blue light, which is thought to be regulated by a BLUF protein, BlsA. To understand the molecular mechanism of light sensing, we have used steady-state and ultrafast vibrational spectroscopy to compare the photoactivation mechanism of BlsA to the BLUF photosensor AppA from Rhodobacter sphaeroides. Although similar photocycles are observed, vibrational data together with homology modeling identify significant differences in the β5 strand in BlsA caused by photoactivation, which are proposed to be directly linked to downstream signaling.
Original languageEnglish
Pages (from-to)220-224
Number of pages5
JournalThe Journal of Physical Chemistry Letters
Issue number1
Publication statusPublished - 2 Jan 2014


  • blue light using FAD
  • BLUF domain
  • BlsA
  • photosensor
  • Acinetobacter baumannii
  • ultrafast time-resolved infrared
  • AppA

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