1a5o
From Proteopedia
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K217C 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
1A5O is a [Protein complex] structure of sequences from [Klebsiella aerogenes] with NI and FMT as [ligands]. Active as [Urease], with EC number [3.5.1.5]. Structure known Active Sites: ACT and NIL. 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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