Ultrafast Structural Dynamics of BlsA, a Photoreceptor from the Pathogenic Bacterium Acinetobacter baumannii.

Ultrafast Structural Dynamics of BlsA, a Photoreceptor from the Pathogenic Bacterium Acinetobacter baumannii.
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DOI:
10.1021/jz4023738
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发表时间:
2014-01-02
期刊:
The journal of physical chemistry letters
影响因子:
--
通讯作者:
Tonge PJ
Tonge PJ
中科院分区:
其他
文献类型:
--
作者:
Brust R;Haigney A;Lukacs A;Gil A;Hossain S;Addison K;Lai CT;Towrie M;Greetham GM;Clark IP;Illarionov B;Bacher A;Kim RR;Fischer M;Simmerling C;Meech SR;Tonge PJ

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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.
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