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[[Image:2boo.gif|left|200px]]<br />
<applet load="2boo" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2boo, resolution 1.80&Aring;" />
'''THE CRYSTAL STRUCTURE OF URACIL-DNA N-GLYCOSYLASE (UNG) FROM DEINOCOCCUS RADIODURANS.'''<br />


==Overview==
==The crystal structure of Uracil-DNA N-Glycosylase (UNG) from Deinococcus radiodurans.==
Uracil-DNA glycosylases are DNA-repair enzymes that catalyse the removal, of promutagenic uracil from single- and double-stranded DNA, thereby, initiating the base-excision repair (BER) pathway. Uracil in DNA can occur, by mis-incorporation of dUMP in place of dTMP during DNA synthesis or by, deamination of cytosine, resulting in U-A or U-G mispairs. The, radiation-resistant bacterium Deinococcus radiodurans has an elevated, number of uracil-DNA glycosylases compared with most other organisms. The, crystal structure of dr0689 (uracil-DNA N-glycosylase), which has been, shown to be the major contributor to the removal of mis-incorporated, uracil bases in crude cell extracts of D. radiodurans, is reported.
<StructureSection load='2boo' size='340' side='right'caption='[[2boo]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2boo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans_R1 Deinococcus radiodurans R1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BOO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BOO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2boo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2boo OCA], [https://pdbe.org/2boo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2boo RCSB], [https://www.ebi.ac.uk/pdbsum/2boo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2boo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/UNG_DEIRA UNG_DEIRA] Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bo/2boo_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2boo ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Uracil-DNA glycosylases are DNA-repair enzymes that catalyse the removal of promutagenic uracil from single- and double-stranded DNA, thereby initiating the base-excision repair (BER) pathway. Uracil in DNA can occur by mis-incorporation of dUMP in place of dTMP during DNA synthesis or by deamination of cytosine, resulting in U-A or U-G mispairs. The radiation-resistant bacterium Deinococcus radiodurans has an elevated number of uracil-DNA glycosylases compared with most other organisms. The crystal structure of dr0689 (uracil-DNA N-glycosylase), which has been shown to be the major contributor to the removal of mis-incorporated uracil bases in crude cell extracts of D. radiodurans, is reported.


==About this Structure==
Structure of the uracil-DNA N-glycosylase (UNG) from Deinococcus radiodurans.,Leiros I, Moe E, Smalas AO, McSweeney S Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1049-56. Epub 2005, Jul 20. PMID:16041069<ref>PMID:16041069</ref>
2BOO 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 NO3 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Hydrolase Hydrolase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.3 3.2.2.3]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BOO OCA]].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure of the uracil-DNA N-glycosylase (UNG) from Deinococcus radiodurans., Leiros I, Moe E, Smalas AO, McSweeney S, Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1049-56. Epub 2005, Jul 20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16041069 16041069]
</div>
[[Category: Deinococcus radiodurans]]
<div class="pdbe-citations 2boo" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
[[Category: Leiros, I.]]
[[Category: Mcsweeney, S.]]
[[Category: Moe, E.]]
[[Category: Smalas, A.O.]]
[[Category: NO3]]
[[Category: base excision repair]]
[[Category: deinococcus radiodurans]]
[[Category: dna damage]]
[[Category: dna repair]]
[[Category: glycosidase]]
[[Category: hydrolase]]
[[Category: radiation resistance]]
[[Category: ung]]
[[Category: uracil-dna glycosylase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:23:37 2007''
==See Also==
*[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Deinococcus radiodurans R1]]
[[Category: Large Structures]]
[[Category: Leiros I]]
[[Category: McSweeney S]]
[[Category: Moe E]]
[[Category: Smalas AO]]

Latest revision as of 13:50, 13 December 2023

The crystal structure of Uracil-DNA N-Glycosylase (UNG) from Deinococcus radiodurans.

2boo, resolution 1.80Å

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