1yql

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Revision as of 18:17, 12 November 2007

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spinqualitylabelsall models 1yql, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Catalytically inactive hOGG1 crosslinked with 7-deaza-8-azaguanine containing DNA

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

How DNA repair proteins distinguish between the rare sites of damage and, the vast expanse of normal DNA is poorly understood. Recognizing the, mutagenic lesion 8-oxoguanine (oxoG) represents an especially formidable, challenge, because this oxidized nucleobase differs by only two atoms from, its normal counterpart, guanine (G). Here we report the use of a covalent, trapping strategy to capture a human oxoG repair protein, 8-oxoguanine DNA, glycosylase I (hOGG1), in the act of interrogating normal DNA. The X-ray, structure of the trapped complex features a target G nucleobase extruded, from the DNA helix but denied insertion into the lesion recognition pocket, of the enzyme. Free energy difference calculations show that both, attractive and repulsive interactions have an important role in the, preferential binding of oxoG compared with G to the active site. The, structure reveals a remarkably effective gate-keeping strategy for lesion, discrimination and suggests a mechanism for oxoG insertion into the hOGG1, active site.

Disease

Known disease associated with this structure: Renal cell carcinoma, clear cell, somatic OMIM:[601982]

About this Structure

1YQL is a Single protein structure of sequence from Homo sapiens with CA as ligand. Full crystallographic information is available from OCA.

Reference

Structure of a repair enzyme interrogating undamaged DNA elucidates recognition of damaged DNA., Banerjee A, Yang W, Karplus M, Verdine GL, Nature. 2005 Mar 31;434(7033):612-8. PMID:15800616

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