Crystal structure of transaldolase B from Escherichia coli suggests a circular permutation of the α/β barrel within the class I aldolase family

Structure

Volumn 4, Issue 6, 1996, Pages 715-724

  Jia, Jia ^a   Huang, Weijun ^a   Schörken, Ulrich ^b   Sahm, Hermann ^b   Sprenger, Georg A ^b   Lindqvist, Ylva ^a   Schneider, Gunter ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

^b FORSCHUNGSZENTRUM JÜLICH   (Germany)

Author keywords

Enzyme mechanism; Evolution; Gene permutation; Protein crystallography; Transaldolase

Indexed keywords

ESCHERICHIA COLI;

FRUCTOSE BISPHOSPHATE ALDOLASE; SCHIFF BASE; TRANSALDOLASE;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; CLASSIFICATION; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; METABOLISM; MOLECULAR EVOLUTION; MOLECULAR GENETICS; PENTOSE PHOSPHATE CYCLE; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; SEQUENCE ALIGNMENT; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; EVOLUTION, MOLECULAR; FRUCTOSE-BISPHOSPHATE ALDOLASE; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PENTOSE PHOSPHATE PATHWAY; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SCHIFF BASES; SEQUENCE ALIGNMENT; TRANSALDOLASE;

EID: 0030585419     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00077-9     Document Type: Article

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