The 1.25 Å resolution structure of phosphoribosyl-ATP pyrophosphohydrolase from Mycobacterium tuberculosis

Acta Crystallographica Section D: Biological Crystallography

Volumn 64, Issue 6, 2008, Pages 627-635

  Javid Majd, Farah ^a   Yang, Dong ^a   Ioerger, Thomas R ^a   Sacchettini, James C ^a  

^a TEXAS A AND M UNIVERSITY   (United States)

Author keywords

Actinobacteria; Catalytic mechanism; Histidine biosynthesis; Pyrophosphatase; Tuberculosis

Indexed keywords

ACTINOBACTERIA; ARCHAEA; BACTERIA (MICROORGANISMS); CAMPYLOBACTER JEJUNI; FUNGI; MYCOBACTERIUM TUBERCULOSIS;

APOENZYME; INORGANIC PYROPHOSPHATASE; PHOSPHORIBOSYL ATP PYROPHOSPHATASE; PHOSPHORIBOSYL-ATP PYROPHOSPHATASE;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS CEREUS; BACTERIAL GENE; CHEMICAL STRUCTURE; CHEMISTRY; CHROMOBACTERIUM; DIMERIZATION; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETICS; MOLECULAR GENETICS; MYCOBACTERIUM TUBERCULOSIS; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY; SPECIES DIFFERENCE; STREPTOMYCES COELICOLOR; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; APOENZYMES; BACILLUS CEREUS; CATALYTIC DOMAIN; CHROMOBACTERIUM; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; GENES, BACTERIAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MYCOBACTERIUM TUBERCULOSIS; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PYROPHOSPHATASES; SEQUENCE HOMOLOGY, AMINO ACID; SPECIES SPECIFICITY; STREPTOMYCES COELICOLOR;

EID: 45749154190     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444908007105     Document Type: Article

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