Crystal structure of decameric fructose-6-phosphate aldolase from Escherichia coli reveals inter-subunit helix swapping as a structural basis for assembly differences in the transaldolase family

Journal of Molecular Biology

Volumn 319, Issue 1, 2002, Pages 161-171

  Thorell, Stina ^a   Schürmann, Melanie ^b   Sprenger, Georg A ^b   Schneider, Gunter ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

^b FORSCHUNGSZENTRUM JÜLICH   (Germany)

Author keywords

Aldolase; Domain swapping; Enzyme mechanism; Protein crystallography; Transaldolase

Indexed keywords

DIMER; FRUCTOSE 6 PHOSPHATE; FRUCTOSE BISPHOSPHATE ALDOLASE; GLYCERALDEHYDE; LYSINE; PROTEIN SUBUNIT; TRANSALDOLASE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; ESCHERICHIA COLI; GENE DELETION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; MAMMALIA;

EID: 0036304877     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00258-9     Document Type: Article

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