Active site conformational changes upon reaction intermediate biotinyl-5'-AMP binding in biotin protein ligase from Mycobacterium tuberculosis

Protein Science

Volumn 23, Issue 7, 2014, Pages 932-939

  Ma, Qingjun ^a   Akhter, Yusuf ^a   Wilmanns, Matthias ^a   Ehebauer, Matthias T ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

Biotinylation; Bira; BPL; Crystal structure; Mycobacterium tuberculosis

Indexed keywords

ADENOSINE PHOSPHATE; BACTERIAL ENZYME; BIOTIN PROTEIN LIGASE; BIOTINYL 5 AMP; LYSINE; SERINE; UNCLASSIFIED DRUG; 5'-AMP-BIOTIN; BACTERIAL PROTEIN; BIOTIN; LIGASE;

ARTICLE; BACTERIAL CELL WALL; BIOTINYLATION; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME STRUCTURE; GEL FILTRATION; LIGAND BINDING; MOLECULAR WEIGHT; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN SECONDARY STRUCTURE; ANALOGS AND DERIVATIVES; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; METABOLISM; PROTEIN CONFORMATION; PROTEIN MOTIF; X RAY CRYSTALLOGRAPHY;

ADENOSINE MONOPHOSPHATE; AMINO ACID MOTIFS; BACTERIAL PROTEINS; BIOTIN; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; LIGASES; LYSINE; MODELS, MOLECULAR; MYCOBACTERIUM TUBERCULOSIS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY;

EID: 84904170635     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2475     Document Type: Article

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