1mug: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /><applet load="1mug" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mug, resolution 1.80Å" /> '''G:T/U MISMATCH-SPECI...
 
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1mug.gif|left|200px]]<br /><applet load="1mug" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1mug.gif|left|200px]]<br /><applet load="1mug" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1mug, resolution 1.80&Aring;" />
caption="1mug, resolution 1.80&Aring;" />
'''G:T/U MISMATCH-SPECIFIC DNA GLYCOSYLASE FROM E.COLI'''<br />
'''G:T/U MISMATCH-SPECIFIC DNA GLYCOSYLASE FROM E.COLI'''<br />


==Overview==
==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.
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==
1MUG 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 SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MUG OCA].  
1MUG 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=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUG OCA].  


==Reference==
==Reference==
Line 14: Line 14:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Barlow, T.]]
[[Category: Barlow, T.]]
[[Category: Barrett, T.E.]]
[[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.H.]]
[[Category: Pearl, L H.]]
[[Category: Savva, R.]]
[[Category: Savva, R.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: dna-glycosylase]]
[[Category: dna-glycosylase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:42:33 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:59:06 2008''