2c2p
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2c2p.gif|left|200px]]<br /><applet load="2c2p" size=" | + | [[Image:2c2p.gif|left|200px]]<br /><applet load="2c2p" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2c2p, resolution 1.75Å" /> | caption="2c2p, resolution 1.75Å" /> | ||
'''THE CRYSTAL STRUCTURE OF MISMATCH SPECIFIC URACIL-DNA GLYCOSYLASE (MUG) FROM DEINOCOCCUS RADIODURANS'''<br /> | '''THE CRYSTAL STRUCTURE OF MISMATCH SPECIFIC URACIL-DNA GLYCOSYLASE (MUG) FROM DEINOCOCCUS RADIODURANS'''<br /> | ||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2C2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] with ACT as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Act Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2C2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] with <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Act+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C2P OCA]. |
==Reference== | ==Reference== | ||
| Line 26: | Line 26: | ||
[[Category: uracil-dna glycosylase]] | [[Category: uracil-dna glycosylase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:30:40 2008'' |
Revision as of 08:30, 3 February 2008
|
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 with as ligand. Known structural/functional Site: . 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
Page seeded by OCA on Sun Feb 3 10:30:40 2008
