Molecular architecture of the Mn2+-dependent lactonase UlaG reveals an RNase-like metallo-β-lactamase fold and a novel quaternary structure

Journal of Molecular Biology

Volumn 398, Issue 5, 2010, Pages 715-729

  Garces, Fernando ^a,b   Fernández, Francisco José ^c   Montellà, Cristina ^a   Penya Soler, Esther ^b,c   Prohens, Rafel ^a   Aguilar, Juan ^a   Baldomà, Laura ^a   Coll, Miquel ^b,d   Badia, Josefa ^a   Vega, M Cristina ^b,c  

^a UNIVERSITY OF BARCELONA   (Spain)

^b INSTITUT DE BIOLOGIA MOLECULAR DE BARCELONA   (Spain)

^c CENTRO DE INVESTIGACIONES BIOLÓGICAS   (Spain)

^d INSTITUTE FOR RESEARCH IN BIOMEDICINE   (Spain)

Author keywords

Crystal structure; Eubacteria; Evolution; L ascorbate metabolism; Metallo lactamase

Indexed keywords

APOENZYME; ASCORBATE PEROXIDASE; COBALT; CYCLIC NUCLEOTIDE; DNA; GLUCONOLACTONASE; HOLOENZYME; IRON; MANGANESE; METALLO BETA LACTAMASE; PHOSPHODIESTERASE; PROTEIN ULAG; RIBONUCLEASE; UNCLASSIFIED DRUG; ZINC ION; ASCORBIC ACID; BETA LACTAMASE; CARBOXYLESTERASE; ENZYME ACTIVATOR; L ASCORBATE 6 PHOSPHATE LACTONASE, E COLI; L-ASCORBATE 6-PHOSPHATE LACTONASE, E COLI; ZINC;

ARTICLE; BINDING AFFINITY; BINDING SITE; CONTROLLED STUDY; DIFFRACTION; DNA REPAIR; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME DEGRADATION; ENZYME MECHANISM; ENZYME SPECIFICITY; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN QUATERNARY STRUCTURE; STRUCTURAL HOMOLOGY; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; METABOLISM; PROTEIN BINDING; PROTEIN MULTIMERIZATION; X RAY CRYSTALLOGRAPHY;

BACTERIA (MICROORGANISMS); ESCHERICHIA; ESCHERICHIA COLI; KLEBSIELLA; SALMONELLA; SHIGELLA; ULA;

ASCORBIC ACID; BETA-LACTAMASES; CARBOXYLIC ESTER HYDROLASES; CATALYTIC DOMAIN; COBALT; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATORS; ESCHERICHIA COLI; IRON; MANGANESE; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; ZINC;

EID: 77952315424     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.03.041     Document Type: Article

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