1mwi

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(New page: 200px<br /><applet load="1mwi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mwi, resolution 2.35&Aring;" /> '''Crystal structure of...)
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[[Image:1mwi.gif|left|200px]]<br /><applet load="1mwi" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1mwi, resolution 2.35&Aring;" />
caption="1mwi, resolution 2.35&Aring;" />
'''Crystal structure of a MUG-DNA product complex'''<br />
'''Crystal structure of a MUG-DNA product complex'''<br />
==Overview==
==Overview==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MWI OCA].
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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.]]
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[[Category: Barrett, T.E.]]
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[[Category: Barrett, T E.]]
[[Category: Brown, T.]]
[[Category: Brown, T.]]
[[Category: Jiricny, J.]]
[[Category: Jiricny, J.]]
[[Category: Panayotou, G.]]
[[Category: Panayotou, G.]]
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[[Category: Pearl, L.H.]]
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[[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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:45:53 2007''
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''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


1mwi, resolution 2.35Å

Drag the structure with the mouse to rotate

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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