Crystal structure of glutathione synthetase at optimal pH: Domain architecture and structural similarity with other proteins

Protein Engineering

Volumn 9, Issue 12, 1996, Pages 1083-1092

  Matsuda, Keiko ^a   Mizuguchi, Kenji ^a   Nishioka, Takaaki ^a   Kato, Hiroaki ^a   Go, Nobuhiro ^a   Oda, JuN'Ichi ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

ATP binding motif; pH dependent domain movement; Spatial arrangements of secondary structural elements; Structural similarity; X ray crystallography

Indexed keywords

ESCHERICHIA; ESCHERICHIA COLI B;

ACETYL COENZYME A CARBOXYLASE; ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; DEXTRO ALANINE DEXTRO ALANINE LIGASE; DIMER; GLUTATHIONE SYNTHASE; NUCLEOTIDE BINDING PROTEIN; SUCCINYL COENZYME A SYNTHETASE;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; ENZYME CONFORMATION; ENZYME STABILITY; ESCHERICHIA COLI; PH; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY;

ACETYL-COA CARBOXYLASE; ADENOSINE TRIPHOSPHATE; BINDING SITES; COMPUTER SIMULATION; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ESCHERICHIA COLI; GLUTATHIONE SYNTHASE; HYDROGEN-ION CONCENTRATION; LIGASES; MODELS, MOLECULAR; MOTION; PEPTIDE SYNTHASES; PROTEIN CONFORMATION; REPRODUCIBILITY OF RESULTS; SUCCINATE-COA LIGASES;

EID: 0030447825     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/9.12.1083     Document Type: Article

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