A new mode of dimerization of allosteric enzymes with ACT domains revealed by the crystal structure of the aspartate kinase from Cyanobacteria

Journal of Molecular Biology

Volumn 399, Issue 2, 2010, Pages 283-293

  Robin, Adeline Y ^a,b,c,d   Cobessi, David ^e   Curien, Gilles ^a,b,c,d   Robert Genthon, Mylène ^a,b,c,d   Ferrer, Jean Luc ^e   Dumas, Renaud ^a,b,c,d  

^a CNRS   (France)

^b Laboratoire de Physiologie Cellulaire Vegetale Grenoble   (France)

^c UNIV GRENOBLE ALPES   (France)

^d CEMAGREF   (France)

^e INSTITUT DE BIOLOGIE STRUCTURALE   (France)

Author keywords

ACT domain; Allostery; Amino acid; Aspartate kinase; Synechocystis

Indexed keywords

ASPARTATE KINASE; ASPARTATE KINASE ALPHA; ASPARTATE KINASE BETA; BACTERIAL PROTEIN; CHORISMATE MUTASE; LYSINE; PREPHENATE DEHYDROGENASE; PROTEIN ACT; PROTEIN ACT1; PROTEIN ACT2; PROTEIN ACT3; PROTEIN ACT4; THREONINE; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CATALYSIS; CONTROLLED STUDY; CRYSTALLOID; DIMERIZATION; ENZYME ACTIVITY; ENZYME ENGINEERING; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS; SYNECHOCYSTIS;

CYANOBACTERIA; SYNECHOCYSTIS;

EID: 77953597414     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.04.014     Document Type: Article

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