McbR/YncC: Implications for the mechanism of ligand and DNA binding by a bacterial gntr transcriptional regulator involved in biofilm formation

Biochemistry

Volumn 53, Issue 46, 2014, Pages 7223-7231

  Lord, Dana M ^a,b   Uzgoren Baran, Ayse ^b,d   Soo, Valerie W C ^c   Wood, Thomas K ^c   Peti, Wolfgang ^b   Page, Rebecca ^a  

^a BROWN UNIVERSITY   (United States)

^b BROWN UNIVERSITY   (United States)

^c PENNSYLVANIA STATE UNIVERSITY   (United States)

^d HACETTEPE UNIVERSITY   (Turkey)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOLOGY; BINDING SITES; CRYSTAL STRUCTURE; DNA; ESCHERICHIA COLI; GENES; PROTEINS;

BACILLUS SUBTILIS; BIOFILM DEVELOPMENT; BIOFILM FORMATION; C-TERMINAL DOMAINS; EXOPOLYSACCHARIDES; EXPONENTIAL GROWTH; TRANSCRIPTIONAL REGULATOR; TRANSCRIPTIONAL REPRESSORS;

BIOFILMS;

BACTERIAL PROTEIN; EXOPOLYSACCHARIDE; GLUCONIC ACID; MQSR CONTROLLED COLANIC ACID AND BIOFILM REGULATOR; PROTEIN FADR; PROTEIN GNTR; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; BACTERIAL DNA; DNA BINDING PROTEIN; ESCHERICHIA COLI PROTEIN; GNTR PROTEIN, E COLI; MCBR PROTEIN, E COLI; PROTEIN BINDING;

ARTICLE; BACILLUS SUBTILIS; BINDING SITE; BIOFILM; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; DIMERIZATION; DNA BINDING; DNA SEQUENCE; ESCHERICHIA COLI; GENE REPRESSION; LIGAND BINDING; NONHUMAN; OLIGOMERIZATION; OPERON; PROTEIN CONFORMATION; PROTEIN FUNCTION; PROTEIN QUATERNARY STRUCTURE; STRESS; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; GENE EXPRESSION REGULATION; GENETICS; GROWTH, DEVELOPMENT AND AGING; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGY; PROTEIN MULTIMERIZATION; X RAY CRYSTALLOGRAPHY;

BACTERIA (MICROORGANISMS);

AMINO ACID SEQUENCE; BINDING SITES; BIOFILMS; CRYSTALLOGRAPHY, X-RAY; DNA, BACTERIAL; DNA-BINDING PROTEINS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENE EXPRESSION REGULATION, BACTERIAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; TRANSCRIPTION FACTORS;

EID: 84913532140     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500871a     Document Type: Article

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