Ultrafast Structural Dynamics of BlsA, a Photoreceptor from the Pathogenic Bacterium Acinetobacter baumannii.
J Phys Chem Lett
; 5(1): 220-224, 2014 Jan 02.
Article
en En
| MEDLINE
| ID: mdl-24723998
ABSTRACT
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 ß5 strand in BlsA caused by photoactivation, which are proposed to be directly linked to downstream signaling.
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Colección:
01-internacional
Base de datos:
MEDLINE
Idioma:
En
Revista:
J Phys Chem Lett
Año:
2014
Tipo del documento:
Article
País de afiliación:
Estados Unidos