1mug: Difference between revisions
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[[Image:1mug.gif|left|200px]] | [[Image:1mug.gif|left|200px]] | ||
'''G:T/U MISMATCH-SPECIFIC DNA GLYCOSYLASE FROM E.COLI''' | {{Structure | ||
|PDB= 1mug |SIZE=350|CAPTION= <scene name='initialview01'>1mug</scene>, resolution 1.80Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''G:T/U MISMATCH-SPECIFIC DNA GLYCOSYLASE FROM E.COLI''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1MUG is a [ | 1MUG is a [[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=1MUG OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9489705 9489705] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: dna-glycosylase]] | [[Category: dna-glycosylase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:48:16 2008'' | ||
Revision as of 10:48, 20 March 2008
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| 1mug, resolution 1.80Å | |||||||||||||
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| Ligands: | SO4 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
G:T/U MISMATCH-SPECIFIC DNA GLYCOSYLASE FROM E.COLI
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
1MUG 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
Page seeded by OCA on Thu Mar 20 12:48:16 2008
