The structure of a reduced form of OxyR from Neisseria meningitidis

BMC Structural Biology

Volumn 10, Issue , 2010, Pages

  Sainsbury, Sarah ^a   Ren, Jingshan ^a   Nettleship, Joanne E ^a   Saunders, Nigel J ^b   Stuart, David I ^a   Owens, Raymond J ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE DERIVATIVE; DIMER; TETRAMER; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR OXYR; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CYSTEINE; DNA; REPRESSOR PROTEIN;

ARTICLE; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; DISULFIDE BOND; DNA BINDING MOTIF; ESCHERICHIA COLI; NEISSERIA MENINGITIDIS; NONHUMAN; OXIDATION REDUCTION POTENTIAL; OXIDATION REDUCTION STATE; OXIDATIVE STRESS; PROTEIN ANALYSIS; PROTEIN DNA BINDING; PROTEIN DNA INTERACTION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN QUATERNARY STRUCTURE; PROTEIN STRUCTURE; SPECIES DIFFERENCE; STRUCTURAL HOMOLOGY; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; OXIDATION REDUCTION REACTION; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS; X RAY CRYSTALLOGRAPHY;

NEISSERIA; NEISSERIA MENINGITIDIS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; DNA; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NEISSERIA MENINGITIDIS; OXIDATION-REDUCTION; PROTEIN STRUCTURE, TERTIARY; REPRESSOR PROTEINS; SEQUENCE ALIGNMENT;

EID: 77952180202     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-10-10     Document Type: Article

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