1mun: Difference between revisions

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New page: left|200px<br /><applet load="1mun" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mun, resolution 1.2Å" /> '''CATALYTIC DOMAIN OF M...
 
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[[Image:1mun.gif|left|200px]]<br /><applet load="1mun" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1mun.gif|left|200px]]<br /><applet load="1mun" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1mun, resolution 1.2&Aring;" />
caption="1mun, resolution 1.2&Aring;" />
'''CATALYTIC DOMAIN OF MUTY FROM ESCHERICHIA COLI D138N MUTANT'''<br />
'''CATALYTIC DOMAIN OF MUTY FROM ESCHERICHIA COLI D138N MUTANT'''<br />


==Overview==
==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.
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==
==About this Structure==
1MUN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SF4, IMD and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MUN OCA].  
1MUN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SF4:'>SF4</scene>, <scene name='pdbligand=IMD:'>IMD</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUN OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Guan, Y.]]
[[Category: Guan, Y.]]
[[Category: Tainer, J.A.]]
[[Category: Tainer, J A.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: IMD]]
[[Category: IMD]]
[[Category: SF4]]
[[Category: SF4]]
[[Category: dna g.a mismatch repair enzyme]]
[[Category: dna g a mismatch repair enzyme]]
[[Category: dna repair]]
[[Category: dna repair]]
[[Category: glycosidase]]
[[Category: glycosidase]]
[[Category: hydrolase]]
[[Category: hydrolase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:42:52 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:59:08 2008''