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3fpn
From Proteopedia
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| - | [[Image:3fpn.png|left|200px]] | ||
| - | < | + | ==Crystal structure of UvrA-UvrB interaction domains== |
| - | + | <StructureSection load='3fpn' size='340' side='right'caption='[[3fpn]], [[Resolution|resolution]] 1.80Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[3fpn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FPN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FPN 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]] 1.8Å</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=3fpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fpn OCA], [https://pdbe.org/3fpn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fpn RCSB], [https://www.ebi.ac.uk/pdbsum/3fpn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fpn ProSAT]</span></td></tr> |
| - | + | </table> | |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/D0VX13_GEOSE D0VX13_GEOSE] | ||
| + | == 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/fp/3fpn_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=3fpn ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Nucleotide excision repair is distinguished from other DNA repair pathways by its ability to process a wide range of structurally unrelated DNA lesions. In bacteria, damage recognition is achieved by the UvrA.UvrB ensemble. Here, we report the structure of the complex between the interaction domains of UvrA and UvrB. These domains are necessary and sufficient for full-length UvrA and UvrB to associate and thereby form the DNA damage-sensing complex of bacterial nucleotide excision repair. The crystal structure and accompanying biochemical analyses suggest a model for the complete damage-sensing complex. | ||
| - | + | A structural model for the damage-sensing complex in bacterial nucleotide excision repair.,Pakotiprapha D, Liu Y, Verdine GL, Jeruzalmi D J Biol Chem. 2009 May 8;284(19):12837-44. Epub 2009 Mar 13. PMID:19287003<ref>PMID:19287003</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3fpn" style="background-color:#fffaf0;"></div> | |
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| - | == | + | |
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==See Also== | ==See Also== | ||
| - | *[[ | + | *[[UvrABC|UvrABC]] |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | |
| - | < | + | |
[[Category: Geobacillus stearothermophilus]] | [[Category: Geobacillus stearothermophilus]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Jeruzalmi D]] |
| - | [[Category: | + | [[Category: Pakotiprapha D]] |
| - | [[Category: | + | [[Category: Verdine GL]] |
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Current revision
Crystal structure of UvrA-UvrB interaction domains
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