2jhq

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[[Image:2jhq.png|left|200px]]
 
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==Crystal structure of Uracil DNA-glycosylase from Vibrio cholerae==
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The line below this paragraph, containing "STRUCTURE_2jhq", creates the "Structure Box" on the page.
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<StructureSection load='2jhq' size='340' side='right'caption='[[2jhq]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2jhq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JHQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JHQ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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{{STRUCTURE_2jhq| PDB=2jhq | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jhq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jhq OCA], [https://pdbe.org/2jhq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jhq RCSB], [https://www.ebi.ac.uk/pdbsum/2jhq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jhq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/UNG_VIBCH UNG_VIBCH] 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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jh/2jhq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2jhq ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystal structure of Vibrio cholerae uracil-DNA N-glycosylase (vcUNG) has been determined to 1.5 A resolution. Based on this structure, a homology model of Aliivibrio salmonicida uracil-DNA N-glycosylase (asUNG) was built. A previous study demonstrated that asUNG possesses typical cold-adapted features compared with vcUNG, such as a higher catalytic efficiency owing to increased substrate affinity. Specific amino-acid substitutions in asUNG were suggested to be responsible for the increased substrate affinity and the elevated catalytic efficiency by increasing the positive surface charge in the DNA-binding region. The temperature adaptation of these enzymes has been investigated using structural and mutational analyses, in which mutations of vcUNG demonstrated an increased substrate affinity that more resembled that of asUNG. Visualization of surface potentials revealed a more positive potential for asUNG compared with vcUNG; a modelled double mutant of vcUNG had a potential around the substrate-binding region that was more like that of asUNG, thus rationalizing the results obtained from the kinetic studies.
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===Crystal structure of Uracil DNA-glycosylase from Vibrio cholerae===
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Structure of uracil-DNA N-glycosylase (UNG) from Vibrio cholerae: mapping temperature adaptation through structural and mutational analysis.,Raeder IL, Moe E, Willassen NP, Smalas AO, Leiros I Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Feb 1;66(Pt 2):130-6. Epub, 2010 Jan 26. PMID:20124707<ref>PMID:20124707</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_20124707}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2jhq" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20124707 is the PubMed ID number.
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{{ABSTRACT_PUBMED_20124707}}
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==About this Structure==
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[[2jhq]] is a 1 chain structure of [[DNA glycosylate]] with sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JHQ OCA].
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==See Also==
==See Also==
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*[[DNA glycosylate|DNA glycosylate]]
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*[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:020124707</ref><references group="xtra"/>
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__TOC__
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[[Category: Uridine nucleosidase]]
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Vibrio cholerae]]
[[Category: Vibrio cholerae]]
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[[Category: Leiros, I.]]
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[[Category: Leiros I]]
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[[Category: Moe, E.]]
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[[Category: Moe E]]
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[[Category: Raeder, I L.U.]]
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[[Category: Raeder ILU]]
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[[Category: Smalas, A O.]]
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[[Category: Smalas AO]]
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[[Category: Willassen, N P.]]
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[[Category: Willassen NP]]
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[[Category: Cold adaptation]]
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[[Category: Dna damage]]
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[[Category: Dna repair]]
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[[Category: Glycosidase]]
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[[Category: Hydrolase]]
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[[Category: Mutational analysis]]
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[[Category: Psychrophilic enzyme]]
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[[Category: Ung]]
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[[Category: Uracil-dna n-glycosylase]]
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[[Category: Vibrio salmonicida]]
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Current revision

Crystal structure of Uracil DNA-glycosylase from Vibrio cholerae

PDB ID 2jhq

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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