Direct contacts between conserved motifs of different subunits provide major contribution to active site organization in human and mycobacterial dUTPases

FEBS Letters

Volumn 584, Issue 14, 2010, Pages 3047-3054

  Takács, Eniko ^a   Nagy, Gergely ^a   Leveles, Ibolya ^a   Harmat, Veronika ^b   Lopata, Anna ^a   Tóth, Judit ^a   Vértessy, Beáta G ^a,c  

^a INSTITUTE OF ENZYMOLOGY   (Hungary)

^b INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^c BUDAPEST UNIVERSITY OF TECHNOLOGY AND ECONOMICS   (Hungary)

Author keywords

Asparagine; Aspartate; DNA repair; DUTPase; Mycobacterium tuberculosis; Nucleotide hydrolysis; Oligomer

Indexed keywords

ASPARAGINE; ASPARTIC ACID; DEOXYURIDINE TRIPHOSPHATE PYROPHOSPHATASE; MAGNESIUM ION; BACTERIAL PROTEIN; DUTP PYROPHOSPHATASE; INORGANIC PYROPHOSPHATASE;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME STRUCTURE; ENZYME SUBUNIT; GENE MUTATION; HUMAN; LIGAND BINDING; MUTANT; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN MOTIF; STEADY STATE; WILD TYPE; BINDING SITE; GENETICS; KINETICS; METABOLISM; PROTEIN TERTIARY STRUCTURE;

MYCOBACTERIUM TUBERCULOSIS;

AMINO ACID MOTIFS; BACTERIAL PROTEINS; BINDING SITES; HUMANS; KINETICS; PROTEIN STRUCTURE, TERTIARY; PYROPHOSPHATASES;

EID: 77954176750     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.05.018     Document Type: Article

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