X-Ray Crystallographic Studies of Hemk from Thermotoga maritima, an N5-Glutamine Methyltransferase

The enzyme HemK (or PrmC) is one of the first identified methyltransferases that modify glutamine. It methylates the highly conserved GGQ motif in class I release factors (RF1 and RF2) in Escherichia coli. HemK from Thermotoga maritima was over-expressed and crystallized in the presence of S-adensyl...

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Veröffentlicht in:	Molecules and cells 2003, 16(2), , pp.266-269
Hauptverfasser:	Yoon, H.J, Kang, K.A, Ahn, H.J, Shim, S.M, Ha, J.Y, Lee, S.K, Suh, S.W. (Seoul National University, Seoul, Republic of Korea), Mikami, B. (Kyoto University, Kyoto, Japan)
Format:	Artikel
Sprache:	eng
Schlagworte:	Crystallization Crystallography, X-Ray Escherichia coli - genetics Escherichia coli Proteins - chemistry GLUTAMINE Glutamine - chemistry Methyltransferases - chemistry Protein Methyltransferases - chemistry Recombinant Proteins - chemistry Thermotoga maritima - chemistry 생물학
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Beschreibung
Zusammenfassung:	The enzyme HemK (or PrmC) is one of the first identified methyltransferases that modify glutamine. It methylates the highly conserved GGQ motif in class I release factors (RF1 and RF2) in Escherichia coli. HemK from Thermotoga maritima was over-expressed and crystallized in the presence of S-adensylmethionine at 296 K using ammonium sulfate as the precipitant.
ISSN:	1016-8478 0219-1032
DOI:	10.1016/S1016-8478(23)13799-X