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

Brust, Richard, Haigney, Allison, Lukacs, Andras, Gil, Agnieszka, Hossain, Shahrier, Addison, Kiri, Lai, Cheng-Tsung, Towrie, Michael, Greetham, Gregory M., Clark, Ian P., Illarionov, Boris, Bacher, Adelbert, Kim, Ryu-Ryun, Fischer, Markus, Simmerling, Carlos, Meech, Stephen R. ORCID: https://orcid.org/0000-0001-5561-2782 and Tonge, Peter J. (2014) Ultrafast structural dynamics of BlsA, a photoreceptor from the pathogenic bacterium Acinetobacter baumannii. The Journal of Physical Chemistry Letters, 5 (1). pp. 220-224. ISSN 1948-7185

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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.

Item Type: Article
Uncontrolled Keywords: blue light using fad,bluf domain,blsa,photosensor,acinetobacter baumannii,ultrafast time-resolved infrared,appa
Faculty \ School: Faculty of Science > School of Chemistry
Faculty of Science
UEA Research Groups: Faculty of Science > Research Groups > Physical and Analytical Chemistry (former - to 2017)
Faculty of Science > Research Groups > Chemistry of Light and Energy
Faculty of Science > Research Groups > Centre for Photonics and Quantum Science
Depositing User: Pure Connector
Date Deposited: 03 Feb 2014 11:04
Last Modified: 19 Oct 2023 01:16
URI: https://ueaeprints.uea.ac.uk/id/eprint/47479
DOI: 10.1021/jz4023738


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