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1mug
From Proteopedia
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|PDB= 1mug |SIZE=350|CAPTION= <scene name='initialview01'>1mug</scene>, resolution 1.80Å | |PDB= 1mug |SIZE=350|CAPTION= <scene name='initialview01'>1mug</scene>, resolution 1.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mug OCA], [http://www.ebi.ac.uk/pdbsum/1mug PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mug RCSB]</span> | ||
}} | }} | ||
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[[Category: Pearl, L H.]] | [[Category: Pearl, L H.]] | ||
[[Category: Savva, R.]] | [[Category: Savva, R.]] | ||
| - | [[Category: SO4]] | ||
[[Category: dna-glycosylase]] | [[Category: dna-glycosylase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:21:14 2008'' |
Revision as of 19:21, 30 March 2008
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| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Sun Mar 30 22:21:14 2008
