1azo

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1azo, resolution 1.70Å

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DNA MISMATCH REPAIR PROTEIN MUTH FROM E. COLI

Overview

MutS, MutL and MutH are the three essential proteins for initiation of, methyl-directed DNA mismatch repair to correct mistakes made during DNA, replication in Escherichia coli. MutH cleaves a newly synthesized and, unmethylated daughter strand 5' to the sequence d(GATC) in a, hemi-methylated duplex. Activation of MutH requires the recognition of a, DNA mismatch by MutS and MutL. We have crystallized MutH in two space, groups and solved the structures at 1.7 and 2.3 A resolution, respectively. The active site of MutH is located at an interface between, two subdomains that pivot relative to one another, as revealed by, comparison of the crystal structures, and this presumably regulates the, nuclease activity. The relative motion of the two subdomains in MutH, correlates with the position of a protruding C-terminal helix. This helix, appears to act as a molecular lever through which MutS and MutL may, communicate the detection of a DNA mismatch and activate MutH. With, sequence homology to Sau3AI and structural similarity to PvuII, endonuclease, MutH is clearly related to these enzymes by divergent, evolution, and this suggests that type II restriction endonucleases, evolved from a common ancestor.

About this Structure

1AZO is a Single protein structure of sequence from Escherichia coli with EDO as ligand. Full crystallographic information is available from OCA.

Reference

Structural basis for MutH activation in E.coli mismatch repair and relationship of MutH to restriction endonucleases., Ban C, Yang W, EMBO J. 1998 Mar 2;17(5):1526-34. PMID:9482749

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