The crystal structure of Toxoplasma gondii nucleoside triphosphate diphosphohydrolase 1 represents a conformational intermediate in the reductive activation mechanism of the tetrameric enzyme

Proteins: Structure, Function and Bioinformatics

Volumn 81, Issue 7, 2013, Pages 1271-1276

  Krug, Ulrike ^a   Totzauer, Robert ^a   Sträter, Norbert ^a  

^a UNIVERSITY OF LEIPZIG   (Germany)

Author keywords

Crystal packing; Crystal structure; Domain motion; Nucleotidase; Phosphatase

Indexed keywords

DISULFIDE; MICROBIAL ENZYME; MONOMER; NUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 1; UNCLASSIFIED DRUG;

ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; TOXOPLASMA GONDII;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ANTIGENS, CD; APYRASE; CRYSTALLOGRAPHY, X-RAY; HUMANS; KINETICS; MODELS, MOLECULAR; NUCLEOTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; PYROPHOSPHATASES; TOXOPLASMA;

TOXOPLASMA GONDII;

EID: 84879416110     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24288     Document Type: Article

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