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| | <StructureSection load='2jhq' size='340' side='right'caption='[[2jhq]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='2jhq' size='340' side='right'caption='[[2jhq]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jhq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillo_virgola_del_koch"_trevisan_1884 "bacillo virgola del koch" trevisan 1884]. 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 [http://proteopedia.org/fgij/fg.htm?mol=2JHQ FirstGlance]. <br> | + | <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> |
| - | </td></tr><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Uridine_nucleosidase Uridine nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.3 3.2.2.3] </span></td></tr> | + | <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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2jhq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jhq OCA], [http://pdbe.org/2jhq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jhq RCSB], [http://www.ebi.ac.uk/pdbsum/2jhq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jhq ProSAT]</span></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=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> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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). | + | [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). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillo virgola del koch trevisan 1884]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Uridine nucleosidase]] | + | [[Category: Vibrio cholerae]] |
| - | [[Category: Leiros, I]] | + | [[Category: Leiros I]] |
| - | [[Category: Moe, E]] | + | [[Category: Moe E]] |
| - | [[Category: Raeder, I L.U]] | + | [[Category: Raeder ILU]] |
| - | [[Category: Smalas, A O]] | + | [[Category: Smalas AO]] |
| - | [[Category: Willassen, N P]] | + | [[Category: Willassen NP]] |
| - | [[Category: Cold adaptation]]
| + | |
| - | [[Category: Dna damage]]
| + | |
| - | [[Category: Dna repair]]
| + | |
| - | [[Category: Glycosidase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Mutational analysis]]
| + | |
| - | [[Category: Psychrophilic enzyme]]
| + | |
| - | [[Category: Ung]]
| + | |
| - | [[Category: Uracil-dna n-glycosylase]]
| + | |
| - | [[Category: Vibrio salmonicida]]
| + | |
| Structural highlights
Function
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).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Raeder IL, Moe E, Willassen NP, Smalas AO, Leiros I. Structure of uracil-DNA N-glycosylase (UNG) from Vibrio cholerae: mapping temperature adaptation through structural and mutational analysis. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Feb 1;66(Pt 2):130-6. Epub, 2010 Jan 26. PMID:20124707 doi:10.1107/S1744309109052063
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