The β-scaffold of the LOV domain of the brucella light-activated histidine kinase is a key element for signal transduction

Journal of Molecular Biology

Volumn 420, Issue 1-2, 2012, Pages 112-127

  Rinaldi, Jimena ^a   Gallo, Mariana ^a   Klinke, Sebastián ^a   Paris, Gastón ^a   Bonomi, Hernán R ^a   Bogomolni, Roberto A ^b   Cicero, Daniel O ^a   Goldbaum, Fernando A ^a  

^a FUNDACIÓN INSTITUTO LELOIR   (Argentina)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Brucella; histidine kinase; LOV domain; NMR spectroscopy; X ray crystallography

Indexed keywords

PROTEIN HISTIDINE KINASE;

ARTICLE; BRUCELLA ABORTUS; CELLULAR PARAMETERS; CONFORMATIONAL TRANSITION; CRYSTALLIZATION; DARKNESS; DIMERIZATION; HYDROPHOBICITY; LIGHT; LIGHT OXYGEN VOLTAGE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; X RAY CRYSTALLOGRAPHY;

BRUCELLA; BRUCELLA MELITENSIS BIOVAR ABORTUS; PROKARYOTA;

EID: 84861801035     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.04.006     Document Type: Article

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