Structural and functional analysis of the Lmo2642 cyclic nucleotide phosphodiesterase from Listeria monocytogenes

Proteins: Structure, Function and Bioinformatics

Volumn 79, Issue 4, 2011, Pages 1205-1214

  Kim, Yeon Gil ^a   Jeong, Jae Hee ^a   Ha, Nam Chul ^b   Kim, Kyung Jin ^a  

^a Pohang University of Science and Technology (POSTECH)   (South Korea)

^b Pusan National University   (South Korea)

Author keywords

Bacterial pathogen; Crystal structure; Dinuclear center; Enzyme; Metallophosphoesterase

Indexed keywords

ACID PHOSPHATASE TARTRATE RESISTANT ISOENZYME; CYCLIC AMP; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; ESTERASE; IRON; LIPOPROTEIN; LMO2642 PROTEIN; MANGANESE; METALLOPHOSPHOESTERASE; MRE11 PROTEIN; NUCLEAR MATRIX PROTEIN; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; BIOCHEMISTRY; CATALYSIS; CRYSTAL STRUCTURE; ENZYMATIC ASSAY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; HOST CELL; HOST PATHOGEN INTERACTION; LISTERIA MONOCYTOGENES; NONHUMAN; PHAGOSOME; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

ADENINE NUCLEOTIDES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CRYSTALLIZATION; CYCLIC AMP; LISTERIA MONOCYTOGENES; MOLECULAR SEQUENCE DATA; PHOSPHORIC DIESTER HYDROLASES; SEQUENCE ALIGNMENT;

ANIMALIA; BACTERIA (MICROORGANISMS); LISTERIA; LISTERIA MONOCYTOGENES;

EID: 79952483901     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22954     Document Type: Article

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