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1yd2
From Proteopedia
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==Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Thermotoga maritima: Point mutant Y19F bound to the catalytic divalent cation== | ==Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Thermotoga maritima: Point mutant Y19F bound to the catalytic divalent cation== | ||
| - | <StructureSection load='1yd2' size='340' side='right' caption='[[1yd2]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='1yd2' size='340' side='right'caption='[[1yd2]], [[Resolution|resolution]] 1.60Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1yd2]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1yd2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YD2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YD2 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yd2 OCA], [https://pdbe.org/1yd2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yd2 RCSB], [https://www.ebi.ac.uk/pdbsum/1yd2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yd2 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/UVRC_THEMA UVRC_THEMA] The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision (By similarity). |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yd/1yd2_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yd/1yd2_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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=1yd2 ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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==See Also== | ==See Also== | ||
| - | *[[UvrABC|UvrABC]] | + | *[[UvrABC 3D structures|UvrABC 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Thermotoga maritima]] |
| - | [[Category: | + | [[Category: Croteau DL]] |
| - | [[Category: | + | [[Category: DellaVecchia MJ]] |
| - | [[Category: Karakas | + | [[Category: Karakas E]] |
| - | [[Category: Kisker | + | [[Category: Kisker C]] |
| - | [[Category: Rhau | + | [[Category: Rhau B]] |
| - | [[Category: Skorvaga | + | [[Category: Skorvaga M]] |
| - | [[Category: Truglio | + | [[Category: Truglio JJ]] |
| - | [[Category: | + | [[Category: Van Houten B]] |
| - | [[Category: Wang | + | [[Category: Wang H]] |
| - | [[Category: | + | [[Category: Wang L]] |
Current revision
Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Thermotoga maritima: Point mutant Y19F bound to the catalytic divalent cation
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Categories: Large Structures | Thermotoga maritima | Croteau DL | DellaVecchia MJ | Karakas E | Kisker C | Rhau B | Skorvaga M | Truglio JJ | Van Houten B | Wang H | Wang L
