1muy
From Proteopedia
(New page: 200px<br /><applet load="1muy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1muy, resolution 1.4Å" /> '''CATALYTIC DOMAIN OF M...) |
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| - | [[Image:1muy.gif|left|200px]]<br /><applet load="1muy" size=" | + | [[Image:1muy.gif|left|200px]]<br /><applet load="1muy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1muy, resolution 1.4Å" /> | caption="1muy, resolution 1.4Å" /> | ||
'''CATALYTIC DOMAIN OF MUTY FROM ESCHERICHIA COLI'''<br /> | '''CATALYTIC DOMAIN OF MUTY FROM ESCHERICHIA COLI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The DNA glycosylase MutY, which is a member of the Helix-hairpin-Helix | + | 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== | ||
| - | 1MUY 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 GLC, SF4 and IMD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1MUY 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=GLC:'>GLC</scene>, <scene name='pdbligand=SF4:'>SF4</scene> and <scene name='pdbligand=IMD:'>IMD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Guan, Y.]] | [[Category: Guan, Y.]] | ||
| - | [[Category: Tainer, J | + | [[Category: Tainer, J A.]] |
[[Category: GLC]] | [[Category: GLC]] | ||
[[Category: IMD]] | [[Category: IMD]] | ||
[[Category: SF4]] | [[Category: SF4]] | ||
| - | [[Category: dna g | + | [[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:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:59:18 2008'' |
Revision as of 11:59, 21 February 2008
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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 , and 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
Page seeded by OCA on Thu Feb 21 13:59:18 2008
