Crystal structure of reduced MsAcg, a putative nitroreductase from Mycobacterium smegmatis and a close homologue of Mycobacterium tuberculosis Acg

Journal of Biological Chemistry

Volumn 287, Issue 53, 2012, Pages 44372-44383

  Chauviac, François Xavier ^a   Bommer, Martin ^b,c   Yan, Jun ^a,d   Parkin, Gary ^e   Daviter, Tina ^a   Lowden, Philip ^a   Raven, Emma L ^e   Thalassinos, Konstantinos ^a,d   Keep, Nicholas H ^a  

^a UNIVERSITY OF LONDON   (United Kingdom)

^b HUMBOLDT UNIVERSITY   (Germany)

^c HAHN MEITNER INSTITUT   (Germany)

^d UNIVERSITY COLLEGE LONDON   (United Kingdom)

^e UNIVERSITY OF LEICESTER   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BINDING PROTEINS; BIOCHEMICAL PATHWAY; COFACTORS; FLAVIN MONONUCLEOTIDES; GENE DUPLICATIONS; MONOMERIC PROTEINS; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; NAD(P)H; NITROREDUCTASES; RATE OF REACTION;

BACTERIA; DIMERS; ENZYMES; GENES; OXYGEN; PROTEINS; X RAY CRYSTALLOGRAPHY;

TUBES (COMPONENTS);

ACG PROTEIN; BACTERIAL PROTEIN; FLAVINE MONONUCLEOTIDE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CRYSTAL STRUCTURE; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN METABOLISM; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY;

BINDING SITES; CRYSTALLOGRAPHY, X-RAY; FLAVIN MONONUCLEOTIDE; MODELS, MOLECULAR; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; NAD; NADP; NITROREDUCTASES;

MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS;

EID: 84871768426     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.406264     Document Type: Article

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