1yd3: Difference between revisions
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==Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Thermotoga maritima: Point mutant Y43F bound to its catalytic divalent cation== | ==Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Thermotoga maritima: Point mutant Y43F bound to its catalytic divalent cation== | ||
<StructureSection load='1yd3' size='340' side='right' caption='[[1yd3]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='1yd3' size='340' side='right'caption='[[1yd3]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1yd3]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1yd3]] 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=1YD3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YD3 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=1yd3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yd3 OCA], [https://pdbe.org/1yd3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yd3 RCSB], [https://www.ebi.ac.uk/pdbsum/1yd3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yd3 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]] | ||
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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]] | ||