2c2p
From Proteopedia
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|PDB= 2c2p |SIZE=350|CAPTION= <scene name='initialview01'>2c2p</scene>, resolution 1.75Å | |PDB= 2c2p |SIZE=350|CAPTION= <scene name='initialview01'>2c2p</scene>, resolution 1.75Å | ||
|SITE= <scene name='pdbsite=AC1:Act+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Act+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c2p OCA], [http://www.ebi.ac.uk/pdbsum/2c2p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c2p RCSB]</span> | ||
}} | }} | ||
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[[Category: Moe, E.]] | [[Category: Moe, E.]] | ||
[[Category: Smalas, A O.]] | [[Category: Smalas, A O.]] | ||
| - | [[Category: ACT]] | ||
[[Category: deinococcus radioduran]] | [[Category: deinococcus radioduran]] | ||
[[Category: dna repair enzyme]] | [[Category: dna repair enzyme]] | ||
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[[Category: uracil-dna glycosylase]] | [[Category: uracil-dna glycosylase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:15:25 2008'' |
Revision as of 23:15, 30 March 2008
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| , resolution 1.75Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE CRYSTAL STRUCTURE OF MISMATCH SPECIFIC URACIL-DNA GLYCOSYLASE (MUG) FROM DEINOCOCCUS RADIODURANS
Overview
Deinococcus radiodurans is extremely resistant to the effects of ionizing radiation. The source of the radiation resistance is not known, but an expansion of specific protein families related to stress response and damage control has been observed. DNA repair enzymes are among the expanded protein families in D. radiodurans, and genes encoding five different uracil-DNA glycosylases are identified in the genome. Here we report the three-dimensional structure of the mismatch-specific uracil-DNA glycosylase (MUG) from D. radiodurans (drMUG) to a resolution of 1.75 angstroms. Structural analyses suggest that drMUG possesses a novel catalytic residue, Asp-93. Activity measurements show that drMUG has a modified and broadened substrate specificity compared with Escherichia coli MUG. The importance of Asp-93 for activity was confirmed by structural analysis and abolished activity for the mutant drMUGD93A. Two other microorganisms, Bradyrhizobium japonicum and Rhodopseudomonas palustris, possess genes that encode MUGs with the highest sequence identity to drMUG among all of the bacterial MUGs examined. A phylogenetic analysis indicates that these three MUGs form a new MUG/thymidine-DNA glycosylase subfamily, here called the MUG2 family. We suggest that the novel catalytic residue (Asp-93) has evolved to provide drMUG with broad substrate specificity to increase the DNA repair repertoire of D. radiodurans.
About this Structure
2C2P is a Single protein structure of sequence from Deinococcus radiodurans. Full crystallographic information is available from OCA.
Reference
The crystal structure of mismatch-specific uracil-DNA glycosylase (MUG) from Deinococcus radiodurans reveals a novel catalytic residue and broad substrate specificity., Moe E, Leiros I, Smalas AO, McSweeney S, J Biol Chem. 2006 Jan 6;281(1):569-77. Epub 2005 Oct 12. PMID:16223719
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