Structural and functional analysis of Rv3214 from Mycobacterium tuberculosis, a protein with conflicting functional annotations, leads to its characterization as a phosphatase

Journal of Bacteriology

Volumn 188, Issue 10, 2006, Pages 3589-3599

  Watkins, Harriet A ^a   Baker, Edward N ^a  

^a UNIVERSITY OF AUCKLAND   (New Zealand)

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHATASE; PHOSPHOGLYCERATE MUTASE; PROTEIN; PROTEIN RV3214; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME SYNTHESIS; GENE SEQUENCE; GENOME ANALYSIS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; OPEN READING FRAME; PHOSPHATE METABOLISM; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FAMILY; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CONSERVED SEQUENCE; GENOME, BACTERIAL; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MYCOBACTERIUM TUBERCULOSIS; OPEN READING FRAMES; PHOSPHORIC MONOESTER HYDROLASES; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI; MYCOBACTERIUM TUBERCULOSIS;

EID: 33646544698     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.188.10.3589-3599.2006     Document Type: Article

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