2c2p
From Proteopedia
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| - | [[Image:2c2p.gif|left|200px]] | + | [[Image:2c2p.gif|left|200px]] |
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| - | '''THE CRYSTAL STRUCTURE OF MISMATCH SPECIFIC URACIL-DNA GLYCOSYLASE (MUG) FROM DEINOCOCCUS RADIODURANS''' | + | {{Structure |
| + | |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> | ||
| + | |LIGAND= <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''THE CRYSTAL STRUCTURE OF MISMATCH SPECIFIC URACIL-DNA GLYCOSYLASE (MUG) FROM DEINOCOCCUS RADIODURANS''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2C2P is a [ | + | 2C2P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C2P OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16223719 16223719] |
[[Category: Deinococcus radiodurans]] | [[Category: Deinococcus radiodurans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Smalas, A O.]] | [[Category: Smalas, A O.]] | ||
[[Category: ACT]] | [[Category: ACT]] | ||
| - | [[Category: deinococcus | + | [[Category: deinococcus radioduran]] |
| - | [[Category: dna repair | + | [[Category: dna repair enzyme]] |
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: mismatch specific dna-glycosylase]] | [[Category: mismatch specific dna-glycosylase]] | ||
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[[Category: uracil-dna glycosylase]] | [[Category: uracil-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 16:09:59 2008'' |
Revision as of 14:10, 20 March 2008
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| 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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