X-ray crystal structure of TTHB099, a CRP/FNR superfamily transcriptional regulator from thermus thermophilus HB8, reveals a DNA-binding protein with no required allosteric effector molecule

Proteins: Structure, Function and Bioinformatics

Volumn 80, Issue 5, 2012, Pages 1490-1494

  Agari, Yoshihiro ^a   Kuramitsu, Seiki ^a,b   Shinkai, Akeo ^a  

^a Harima Institute ^*  (Japan)

^b OSAKA UNIVERSITY   (Japan)

Author keywords

Functional genomics; Light induced carotenoid biosynthesis; Structural genomics; Thermophile; Transcription factor

Indexed keywords

BACTERIAL PROTEIN; CYCLIC AMP BINDING PROTEIN; DNA BINDING PROTEIN; PROTEIN TTHB099; UNCLASSIFIED DRUG;

ALLOSTERISM; ALPHA HELIX; BETA SHEET; CONTROLLED STUDY; CRYSTAL STRUCTURE; NONHUMAN; NOTE; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; THERMUS THERMOPHILUS;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; CYCLIC AMP RECEPTOR PROTEIN; DNA-BINDING PROTEINS; IRON-SULFUR PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; SEQUENCE ALIGNMENT; THERMUS THERMOPHILUS;

THERMUS THERMOPHILUS;

EID: 84859445057     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24049     Document Type: Note

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