1mwi
From Proteopedia
(New page: 200px<br /><applet load="1mwi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mwi, resolution 2.35Å" /> '''Crystal structure of...) |
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| - | [[Image:1mwi.gif|left|200px]]<br /><applet load="1mwi" size=" | + | [[Image:1mwi.gif|left|200px]]<br /><applet load="1mwi" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mwi, resolution 2.35Å" /> | caption="1mwi, resolution 2.35Å" /> | ||
'''Crystal structure of a MUG-DNA product complex'''<br /> | '''Crystal structure of a MUG-DNA product complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | G:U mismatches resulting from deamination of cytosine are the most common | + | G:U mismatches resulting from deamination of cytosine are the most common promutagenic lesions occurring in DNA. Uracil is removed in a base-excision repair pathway by uracil DNA-glycosylase (UDG), which excises uracil from both single- and double-stranded DNA. Recently, a biochemically distinct family of DNA repair enzymes has been identified, which excises both uracil and thymine, but only from mispairs with guanine. Crystal structures of the mismatch-specific uracil DNA-glycosylase (MUG) from E. coli, and of a DNA complex, reveal a remarkable structural and functional homology to UDGs despite low sequence identity. Details of the MUG structure explain its thymine DNA-glycosylase activity and the specificity for G:U/T mispairs, which derives from direct recognition of guanine on the complementary strand. |
==About this Structure== | ==About this Structure== | ||
| - | 1MWI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1MWI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MWI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Barlow, T.]] | [[Category: Barlow, T.]] | ||
| - | [[Category: Barrett, T | + | [[Category: Barrett, T E.]] |
[[Category: Brown, T.]] | [[Category: Brown, T.]] | ||
[[Category: Jiricny, J.]] | [[Category: Jiricny, J.]] | ||
[[Category: Panayotou, G.]] | [[Category: Panayotou, G.]] | ||
| - | [[Category: Pearl, L | + | [[Category: Pearl, L H.]] |
[[Category: Savva, R.]] | [[Category: Savva, R.]] | ||
[[Category: abasic site]] | [[Category: abasic site]] | ||
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[[Category: nucleotide flipping]] | [[Category: nucleotide flipping]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:59:43 2008'' |
Revision as of 11:59, 21 February 2008
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Crystal structure of a MUG-DNA product complex
Overview
G:U mismatches resulting from deamination of cytosine are the most common promutagenic lesions occurring in DNA. Uracil is removed in a base-excision repair pathway by uracil DNA-glycosylase (UDG), which excises uracil from both single- and double-stranded DNA. Recently, a biochemically distinct family of DNA repair enzymes has been identified, which excises both uracil and thymine, but only from mispairs with guanine. Crystal structures of the mismatch-specific uracil DNA-glycosylase (MUG) from E. coli, and of a DNA complex, reveal a remarkable structural and functional homology to UDGs despite low sequence identity. Details of the MUG structure explain its thymine DNA-glycosylase activity and the specificity for G:U/T mispairs, which derives from direct recognition of guanine on the complementary strand.
About this Structure
1MWI is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions., Barrett TE, Savva R, Panayotou G, Barlow T, Brown T, Jiricny J, Pearl LH, Cell. 1998 Jan 9;92(1):117-29. PMID:9489705
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