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1ux0
From Proteopedia
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BACILLUS SUBTILIS CYTIDINE DEAMINASE WITH AN ARG56- GLN SUBSTITUTION
Overview
The zinc-containing cytidine deaminase (CDA, EC 3.5.4.5) is a pyrimidine, salvage enzyme catalyzing the hydrolytic deamination of cytidine and, 2'-deoxycytidine forming uridine and 2'-deoxyuridine, respectively., Homodimeric CDA (D-CDA) and homotetrameric CDA (T-CDA) both contain one, zinc ion per subunit coordinated to the catalytic water molecule. The zinc, ligands in D-CDA are one histidine and two cysteine residues, whereas in, T-CDA zinc is coordinated to three cysteines. Two of the zinc coordinating, cysteines in T-CDA form hydrogen bonds to the conserved residue Arg56, and, this residue together with the dipole moments from two alpha-helices, partially neutralizes the additional negative charge in the active site, leading to a catalytic activity similar to D-CDA. Arg56 has been, ... [(full description)]
About this Structure
1UX0 is a [Single protein] structure of sequence from [Bacillus subtilis] with ZN and THU as [ligands]. Active as [[1]], with EC number [3.5.4.5]. Full crystallographic information is available from [OCA].
Reference
Structural, kinetic, and mutational studies of the zinc ion environment in tetrameric cytidine deaminase., Johansson E, Neuhard J, Willemoes M, Larsen S, Biochemistry. 2004 May 25;43(20):6020-9. PMID:15147186
Page seeded by OCA on Mon Oct 29 20:20:11 2007
Categories: Bacillus subtilis | Single protein | Johansson, E. | Larsen, S. | Neuhard, J. | Willemoes, M. | THU | ZN | Cdd | Cytidine deaminase | Hydrolase | Pyrimidine metabolism | Salvage | Tetramer | Zinc binding
