Crystal structures of yeast β-alanine synthase complexes reveal the mode of substrate binding and large scale domain closure movements

Journal of Biological Chemistry

Volumn 282, Issue 49, 2007, Pages 36037-36047

  Lundgren, Stina ^a   Andersen, Birgit ^b   Piškur, Jure ^b   Dobritzsch, Doreen ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

^b LUND UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING RESIDUES; METALLOPEPTIDASE-LIKE ENZYME; SUBSTRATE BINDING;

BINDING ENERGY; CRYSTAL STRUCTURE; DIMERIZATION; ENZYMES; HYDROGEN BONDS; MUTAGENESIS;

YEAST;

ARGININE; BETA ALANINE; BETA ALANINE SYNTHASE; FUNGAL ENZYME; GLUTATHIONE; HISTIDINE; METAL; PEPTIDASE; UNCLASSIFIED DRUG; ZINC ION;

ARTICLE; BINDING AFFINITY; CATALYSIS; CRYSTAL STRUCTURE; DIMERIZATION; HYDROGEN BOND; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN INTERACTION; SACCHAROMYCES KLUYVERI; YEAST;

AMIDOHYDROLASES; AMINO ACID SUBSTITUTION; BINDING SITES; CATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; METALLOPROTEASES; MULTIENZYME COMPLEXES; MUTAGENESIS, SITE-DIRECTED; MUTATION, MISSENSE; SACCHAROMYCES; THYMINE; URACIL;

SACCHAROMYCES KLUYVERI;

EID: 37249009047     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M705517200     Document Type: Article

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