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Title

N-acetyi-L-glutamate kinase from Escherichia coli: Cloning of the gene, purification and crystallization of the recombinant enzyme and preliminary X-ray analysis of the free and ligand-bound forms

AuthorsGil-Ortiz, Fernando ; Ramón-Maiques, Santiago ; Marina, Alberto ; Fita, Ignacio ; Rubio, Vicente
Keywordskinases
N-acetyl-L-glutamate kinase
Issue Date1999
PublisherBlackwell Publishing
CitationActa Crystallographica Section D: Biological Crystallography 55(7): 1350-1352 (1999)
AbstractThe gene for Escherichia coli N-acetyl-L-glutamate kinase (NAGK) was cloned in a plasmid and expressed in E. coli, allowing enzyme purification in three steps. NAGK exhibits high specific activity (1.1 μmol s-1 rag-1), lacks Met1 and forms dimers (shown by crosslinking). Crystals of unliganded NAGK diffract to 2 Å and belong to space group P6122 or its enantiomorph P6522 (unit-cell parameters a = b = 78.6, c = 278.0 Å) with two monomers in the asymmetric unit. Crystals of NAGK with acetylglutamate and the ATP analogue AMPPNP diffract to 1.8 Å and belong to space group C2221 (unit-cell parameters a = 60.0, b = 71.9, c = 107.4 Å), with one monomer in the asymmetric unit. NAGK crystallization will allow the determination of proposed structural similarities to carbamate kinase.
Publisher version (URL)http://dx.doi.org/10.1107/S0907444999005351
URIhttp://hdl.handle.net/10261/111140
DOI10.1107/S0907444999005351
Identifiersdoi: 10.1107/S0907444999005351
issn: 0907-4449
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