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1akz

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(New page: 200px<br /> <applet load="1akz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1akz, resolution 1.57&Aring;" /> '''HUMAN URACIL-DNA GL...)
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Revision as of 13:52, 12 November 2007

Image:1akz.gif

1akz, resolution 1.57Å

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HUMAN URACIL-DNA GLYCOSYLASE

Contents

Overview

Crystal structures of the DNA repair enzyme human uracil-DNA glycosylase, (UDG), combined with mutational analysis, reveal the structural basis for, the specificity of the enzyme. Within the classic alpha/beta fold of UDG, sequence-conserved residues form a positively charged, active-site groove, the width of duplex DNA, at the C-terminal edge of the central, four-stranded parallel beta sheet. In the UDG-6-aminouracil complex, uracil binds at the base of the groove within a rigid preformed pocket, that confers selectivity for uracil over other bases by shape, complementary and by main chain and Asn-204 side chain hydrogen bonds., Main chain nitrogen atoms are positioned to stabilize the oxyanion, intermediate generated by His-268 acting via nucleophilic attack or, general base mechanisms. Specific binding of uracil flipped out from a DNA, duplex provides a structural mechanism for damaged base recognition.

Disease

Known diseases associated with this structure: Immunodeficiency with hyper IgM, type 4 OMIM:[191525]

About this Structure

1AKZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis., Mol CD, Arvai AS, Slupphaug G, Kavli B, Alseth I, Krokan HE, Tainer JA, Cell. 1995 Mar 24;80(6):869-78. PMID:7697717

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