Loop-to-helix transition in the structure of multidrug regulator AcrR at the entrance of the drug-binding cavity

Journal of Structural Biology

Volumn 194, Issue 1, 2016, Pages 18-28

  Manjasetty, Babu A ^a,b   Halavaty, Andrei S ^c,d   Luan, Chi Hao ^d,e   Osipiuk, Jerzy ^d,f,g   Mulligan, Rory ^d,f,g   Kwon, Keehwan ^d,h   Anderson, Wayne F ^c,d   Joachimiak, Andrzej ^d,f,g  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (France)

^b UNIV GRENOBLE ALPES   (France)

^c NORTHWESTERN UNIVERSITY   (United States)

^d Center for Structural Genomics of Infectious Diseases (CSGID)   (United States)

^e NORTHWESTERN UNIVERSITY   (United States)

^f UNIVERSITY OF CHICAGO   (United States)

^g ARGONNE NATIONAL LABORATORY   (United States)

^h J CRAIG VENTER INSTITUTE   (United States)

Author keywords

Loop to helix transition; Multidrug resistance; TetR AcrR; Transcription regulator

Indexed keywords

ACRR PROTEIN; CHOLESTEROL; DEQUALINIUM; DIFLUBENZURON; DIMER; ESTRAMUSTINE; FULVESTRANT; IDEBENONE; PRASTERONE; RITONAVIR; TRANSCRIPTION FACTOR; TRICLABENDAZOLE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; LIGAND; PROTEIN BINDING; REPRESSOR PROTEIN;

ALPHA HELIX; ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DRUG BINDING SITE; ESCHERICHIA COLI; HYDROGEN BOND; LIGAND BINDING; LOOP TO HELIX TRANSITION; MOLECULAR DOCKING; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; SALMONELLA ENTERICA SEROVAR TYPHIMURIUM; AMINO ACID SEQUENCE; BINDING SITE; CHEMISTRY; GENETICS; METABOLISM; MOLECULAR CLONING; MOLECULAR MODEL; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; LIGANDS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN DOMAINS; PROTEIN STRUCTURE, SECONDARY; REPRESSOR PROTEINS; SALMONELLA TYPHIMURIUM; SEQUENCE HOMOLOGY, NUCLEIC ACID;

EID: 84958107797     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2016.01.008     Document Type: Article

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