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 1.63&Aring;" /> '''MutM (Fpg) bound to ...)
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[[Image:1r2z.gif|left|200px]]<br /><applet load="1r2z" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1r2z.gif|left|200px]]<br /><applet load="1r2z" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1r2z, resolution 1.63&Aring;" />
caption="1r2z, resolution 1.63&Aring;" />
'''MutM (Fpg) bound to 5,6-dihydrouracil (DHU) containing DNA'''<br />
'''MutM (Fpg) bound to 5,6-dihydrouracil (DHU) containing DNA'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1R2Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1R2Z OCA].
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1R2Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R2Z OCA].
==Reference==
==Reference==
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[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Fromme, J.C.]]
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[[Category: Fromme, J C.]]
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[[Category: Verdine, G.L.]]
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[[Category: Verdine, G L.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: dna glycosylase]]
[[Category: dna glycosylase]]
[[Category: dna repair]]
[[Category: dna repair]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:01:05 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:46:29 2008''

Revision as of 12:46, 21 February 2008


1r2z, resolution 1.63Å

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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 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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