Crystal Structures of the Histidine Acid Phosphatase from Francisella tularensis Provide Insight into Substrate Recognition

Journal of Molecular Biology

Volumn 394, Issue 5, 2009, Pages 893-904

  Singh, Harkewal ^a   Felts, Richard L ^a   Schuermann, Jonathan P ^b   Reilly, Thomas J ^c   Tanner, John J ^a,d  

^a UNIVERSITY OF MISSOURI   (United States)

^b Department of Obstetrics Gynecology   (United States)

^c UNIVERSITY OF MISSOURI   (United States)

^d University of Missouri   (United States)

Author keywords

Francisella tularensis; histidine acid phosphatase; kinetics; substrate recognition; X ray crystallography

Indexed keywords

ACID PHOSPHATASE; ADENOSINE 3' PHOSPHATE; ASPARTIC ACID; HISTIDINE; HISTIDINE ACID PHOSPHATASE; PHOSPHATE; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ANALYSIS; ENZYME INHIBITOR INTERACTION; ENZYME KINETICS; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; FRANCISELLA TULARENSIS; LIGAND BINDING; MACROPHAGE; MOLECULAR INTERACTION; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING;

FRANCISELLA TULARENSIS;

EID: 70449632259     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.10.009     Document Type: Article

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