Two crystal structures of Escherichia coli N-acetyl-l-glutamate kinase demonstrate the cycling between open and closed conformations

Journal of Molecular Biology

Volumn 399, Issue 3, 2010, Pages 476-490

  Gil Ortiz, Fernando ^a   Ramon Maiques, Santiago ^a   Fernandez Murga, Maria L ^a   Fita, Ignacio ^b   Rubio, Vicente ^a  

^a INSTITUTO DE SALUD CARLOS III   (Spain)

^b INSTITUTE FOR RESEARCH IN BIOMEDICINE   (Spain)

Author keywords

Acetylglutamate kinase; Amino acid kinase family; Conformational changes; Phosphoryl group transfer; X ray crystallography

Indexed keywords

ADENOSINE TRIPHOSPHATE; ARGININE; GLUTAMATE ACETYLTRANSFERASE; N ACETYLGLUTAMIC ACID; NUCLEOTIDE; SULFATE;

ARTICLE; BIOSYNTHESIS; CATALYSIS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ESCHERICHIA COLI; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING;

ESCHERICHIA COLI;

EID: 77954759428     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.04.025     Document Type: Article

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