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1okb

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(New page: 200px<br /> <applet load="1okb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1okb, resolution 1.90&Aring;" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 16:21, 29 October 2007

Image:1okb.gif

1okb, resolution 1.90Å

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CRYSTAL STRUCTURE OF URACIL-DNA GLYCOSYLASE FROM ATLANTIC COD (GADUS MORHUA)

Overview

Uracil-DNA glycosylase (UDG; EC 3.2.2.3) is a DNA-repair protein that, catalyses the hydrolysis of promutagenic uracil residues from single- or, double-stranded DNA, generating free uracil and abasic DNA. The crystal, structure of the catalytic domain of cod uracil-DNA glycosylase (cUDG) has, been determined to 1.9 A resolution, with final R factors of 18.61 and, 20.57% for the working and test sets of reflections, respectively. This is, the first crystal structure of a uracil-DNA glycosylase from a, cold-adapted species and a detailed comparison with the human enzyme is, performed in order to rationalize the cold-adapted behaviour of the cod, enzyme at the structural level. The catalytic domain of cUDG comprises 223, residues, with a sequence identity to the human UDG of 75%. The ... [(full description)]

About this Structure

1OKB is a [Single protein] structure of sequence from [Gadus morhua] with CL and GOL as [ligands]. Active as [[1]], with EC number [3.2.2.3]. Full crystallographic information is available from [OCA].

Reference

The structure of uracil-DNA glycosylase from Atlantic cod (Gadus morhua) reveals cold-adaptation features., Leiros I, Moe E, Lanes O, Smalas AO, Willassen NP, Acta Crystallogr D Biol Crystallogr. 2003 Aug;59(Pt 8):1357-65. Epub 2003, Jul 23. PMID:12876336

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