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1muy

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Image:1muy.gif

1muy, resolution 1.4Å

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CATALYTIC DOMAIN OF MUTY FROM ESCHERICHIA COLI

Overview

The DNA glycosylase MutY, which is a member of the Helix-hairpin-Helix, (HhH) DNA glycosylase superfamily, excises adenine from mispairs with, 8-oxoguanine and guanine. High-resolution crystal structures of the MutY, catalytic core (cMutY), the complex with bound adenine, and designed, mutants reveal the basis for adenine specificity and glycosyl bond, cleavage chemistry. The two cMutY helical domains form a, positively-charged groove with the adenine-specific pocket at their, interface. The Watson-Crick hydrogen bond partners of the bound adenine, are substituted by protein atoms, confirming a nucleotide flipping, mechanism, and supporting a specific DNA binding orientation by MutY and, structurally related DNA glycosylases.

About this Structure

1MUY is a Single protein structure of sequence from Escherichia coli with GLC, SF4 and IMD as ligands. Full crystallographic information is available from OCA.

Reference

MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily., Guan Y, Manuel RC, Arvai AS, Parikh SS, Mol CD, Miller JH, Lloyd S, Tainer JA, Nat Struct Biol. 1998 Dec;5(12):1058-64. PMID:9846876

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