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1a5n

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(New page: 200px<br /> <applet load="1a5n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a5n, resolution 2.4&Aring;" /> '''K217A VARIANT OF KLE...)
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Revision as of 18:22, 29 October 2007


1a5n, resolution 2.4Å

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K217A VARIANT OF KLEBSIELLA AEROGENES UREASE, CHEMICALLY RESCUED BY FORMATE AND NICKEL

Overview

Klebsiella aerogenes urease possesses a dinuclear metallocenter in which, two nickel atoms are bridged by carbamylated Lys217. To assess whether, carbamate-specific chemistry is required for urease activity, site-directed mutagenesis and chemical rescue strategies were combined in, efforts to place a carboxylate group at the location of this metal ligand., Urease variants with Lys217 replaced by Glu, Cys, and Ala (K217E, K217C/C319A, and K217A proteins) were purified, shown to be activated by, incubation with small organic acids plus Ni(II), and structurally, characterized. K217C/C319A urease possessed a second change in which, Cys319 was replaced by Ala in order to facilitate efforts to chemically, modify Cys217; however, this covalent modification approach did not, produce active ... [(full description)]

About this Structure

1A5N is a [Protein complex] structure of sequences from [Klebsiella aerogenes] with NI and FMT as [ligands]. Active as [[1]], with EC number [3.5.1.5]. Full crystallographic information is available from [OCA].

Reference

Chemical rescue of Klebsiella aerogenes urease variants lacking the carbamylated-lysine nickel ligand., Pearson MA, Schaller RA, Michel LO, Karplus PA, Hausinger RP, Biochemistry. 1998 Apr 28;37(17):6214-20. PMID:9558361

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