1oe5
From Proteopedia
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|PDB= 1oe5 |SIZE=350|CAPTION= <scene name='initialview01'>1oe5</scene>, resolution 2.30Å | |PDB= 1oe5 |SIZE=350|CAPTION= <scene name='initialview01'>1oe5</scene>, resolution 2.30Å | ||
|SITE= <scene name='pdbsite=AC1:Epe+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Epe+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=DU:2'-DEOXYURIDINE-5'-MONOPHOSPHATE'>DU</scene>, <scene name='pdbligand=DUR:2'-DEOXYURIDINE'>DUR</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=URA:URACIL'>URA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oe5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oe5 OCA], [http://www.ebi.ac.uk/pdbsum/1oe5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oe5 RCSB]</span> | ||
}} | }} | ||
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[[Category: Pearl, L H.]] | [[Category: Pearl, L H.]] | ||
[[Category: Wibley, J E.A.]] | [[Category: Wibley, J E.A.]] | ||
| - | [[Category: DUR]] | ||
| - | [[Category: EPE]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: IPA]] | ||
| - | [[Category: URA]] | ||
[[Category: dna glycosylase]] | [[Category: dna glycosylase]] | ||
[[Category: single stranded]] | [[Category: single stranded]] | ||
[[Category: smug1]] | [[Category: smug1]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:43:57 2008'' |
Revision as of 19:43, 30 March 2008
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| , resolution 2.30Å | |||||||
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| Sites: | |||||||
| Ligands: | , , , , , , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
XENOPUS SMUG1, AN ANTI-MUTATOR URACIL-DNA GLYCOSYLASE
Overview
Cytosine deamination is a major promutagenic process, generating G:U mismatches that can cause transition mutations if not repaired. Uracil is also introduced into DNA via nonmutagenic incorporation of dUTP during replication. In bacteria, uracil is excised by uracil-DNA glycosylases (UDG) related to E. coli UNG, and UNG homologs are found in mammals and viruses. Ung knockout mice display no increase in mutation frequency due to a second UDG activity, SMUG1, which is specialized for antimutational uracil excision in mammalian cells. Remarkably, SMUG1 also excises the oxidation-damage product 5-hydroxymethyluracil (HmU), but like UNG is inactive against thymine (5-methyluracil), a chemical substructure of HmU. We have solved the crystal structure of SMUG1 complexed with DNA and base-excision products. This structure indicates a more invasive interaction with dsDNA than observed with other UDGs and reveals an elegant water displacement/replacement mechanism that allows SMUG1 to exclude thymine from its active site while accepting HmU.
About this Structure
1OE5 is a Protein complex structure of sequences from Xenopus laevis. Full crystallographic information is available from OCA.
Reference
Structure and specificity of the vertebrate anti-mutator uracil-DNA glycosylase SMUG1., Wibley JE, Waters TR, Haushalter K, Verdine GL, Pearl LH, Mol Cell. 2003 Jun;11(6):1647-59. PMID:12820976
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