Crystal structure of D-hydantoinase from Burkholderia pickettii at a resolution of 2.7 Angstroms: Insights into the molecular basis of enzyme thermostability

Journal of Bacteriology

Volumn 185, Issue 14, 2003, Pages 4038-4049

  Xu, Zhen ^a,b   Liu, Yunqing ^a   Yang, Yunliu ^b   Jiang, Weihong ^b   Arnold, Eddy ^c   Ding, Jianping ^a,c  

^a INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

^b INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

^c RUTGERS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIHYDROPYRIMIDINASE;

ARTICLE; BURKHOLDERIA PICKETTII; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME STABILITY; ENZYME STRUCTURE; GEOBACILLUS STEAROTHERMOPHILUS; HYDROGEN BOND; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; STRUCTURE ANALYSIS; THERMOSTABILITY; THERMUS;

AMIDOHYDROLASES; AMINO ACID SEQUENCE; BINDING SITES; BURKHOLDERIA; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ENZYME STABILITY; HYDROPHOBICITY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; TEMPERATURE;

BACTERIA (MICROORGANISMS); BURKHOLDERIA; GEOBACILLUS STEAROTHERMOPHILUS; NEGIBACTERIA; RALSTONIA PICKETTII; THERMUS; THERMUS SP.;

EID: 0038492663     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.14.4038-4049.2003     Document Type: Article

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