Crystal structure of the cellulase Ce19M enlightens structure/function relationships of the variable catalytic modules in glycoside hydrolases

Biochemistry

Volumn 41, Issue 37, 2002, Pages 11134-11142

  Parsiegla, G ^a,b   Belaich A ^a,b   Belaich J P ^a,b   Haser, R ^a,c  

^a CNRS   (France)

^b AIX MARSEILLE UNIVERSITY   (France)

^c UNIVERSITÉ LYON 1   (France)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC MODULES;

BACTERIA; CATALYSIS; CRYSTAL STRUCTURE; SUBSTRATES;

CELLULOSE;

CELLULASE; GLYCOSIDASE; HYDROLASE;

ADAPTATION; ARTICLE; CATALYSIS; CATALYST; CONTROLLED STUDY; COVALENT BOND; CRYSTAL STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CALCIUM; CATALYTIC DOMAIN; CELLULASE; CLOSTRIDIUM; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; GLYCOSIDE HYDROLASES; MOLECULAR SEQUENCE DATA; NICKEL; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP; ZINC;

BACTERIA (MICROORGANISMS);

EID: 0037125924     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi025816m     Document Type: Article

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