1r2z
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(New page: 200px<br /><applet load="1r2z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r2z, resolution 1.63Å" /> '''MutM (Fpg) bound to ...)
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Revision as of 19:53, 24 November 2007
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MutM (Fpg) bound to 5,6-dihydrouracil (DHU) containing DNA
Overview
MutM is a bacterial DNA glycosylase that removes the mutagenic lesion, 8-oxoguanine (oxoG) from duplex DNA. The means of oxoG recognition by MutM, (also known as Fpg) is of fundamental interest, in light of the vast, excess of normal guanine bases present in genomic DNA. The crystal, structure of a recognition-competent but catalytically inactive version of, MutM in complex with oxoG-containing DNA reveals the structural basis for, recognition. MutM binds the oxoG nucleoside in the syn glycosidic, configuration and distinguishes oxoG from guanine by reading out the, protonation state of the N7 atom. The segment of MutM principally, responsible for oxoG recognition is a flexible loop, suggesting that, conformational mobility influences lesion recognition and catalysis., Furthermore, the structure of MutM in complex with DNA containing an, alternative substrate, dihydrouracil, demonstrates how MutM is able to, recognize lesions other than oxoG.
About this Structure
1R2Z is a Single protein structure of sequence from Geobacillus stearothermophilus with ZN as ligand. Full crystallographic information is available from OCA.
Reference
DNA lesion recognition by the bacterial repair enzyme MutM., Fromme JC, Verdine GL, J Biol Chem. 2003 Dec 19;278(51):51543-8. Epub 2003 Oct 1. PMID:14525999
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