1ux0

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spinqualitylabelsall models 1ux0, resolution 1.99Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 [Cytidine deaminase], with EC number [3.5.4.5]. Structure known Active Site: AC1. 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

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