2nrr: Difference between revisions

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-{{Seed}}
-[[Image:2nrr.png|left|200px]]
-<!--
+==Crystal structure of the C-terminal RNAseH endonuclase domain of UvrC==
-The line below this paragraph, containing "STRUCTURE_2nrr", creates the "Structure Box" on the page.
+<StructureSection load='2nrr' size='340' side='right'caption='[[2nrr]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2nrr]] 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=2NRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NRR FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</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=2nrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nrr OCA], [https://pdbe.org/2nrr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nrr RCSB], [https://www.ebi.ac.uk/pdbsum/2nrr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nrr ProSAT]</span></td></tr>
-{{STRUCTURE_2nrr|  PDB=2nrr  |  SCENE=  }}
+</table>
+== 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 ==
+[[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/nr/2nrr_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=2nrr ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Removal and repair of DNA damage by the nucleotide excision repair pathway requires two sequential incision reactions, which are achieved by the endonuclease UvrC in eubacteria. Here, we describe the crystal structure of the C-terminal half of UvrC, which contains the catalytic domain responsible for 5' incision and a helix-hairpin-helix-domain that is implicated in DNA binding. Surprisingly, the 5' catalytic domain shares structural homology with RNase H despite the lack of sequence homology and contains an uncommon DDH triad. The structure also reveals two highly conserved patches on the surface of the protein, which are not related to the active site. Mutations of residues in one of these patches led to the inability of the enzyme to bind DNA and severely compromised both incision reactions. Based on our results, we suggest a model of how UvrC forms a productive protein-DNA complex to excise the damage from DNA.
-===Crystal structure of the C-terminal RNAseH endonuclase domain of UvrC===
+Structure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triad.,Karakas E, Truglio JJ, Croteau D, Rhau B, Wang L, Van Houten B, Kisker C EMBO J. 2007 Jan 24;26(2):613-22. PMID:17245438<ref>PMID:17245438</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2nrr" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_17245438}}, adds the Publication Abstract to the page
+*[[UvrABC|UvrABC]]
-(as it appears on PubMed at http://www.pubmed.gov), where 17245438 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_17245438}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-NRR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NRR OCA].
-==Reference==
-Structure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triad., Karakas E, Truglio JJ, Croteau D, Rhau B, Wang L, Van Houten B, Kisker C, EMBO J. 2007 Jan 24;26(2):613-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17245438 17245438]
-[[Category: Single protein]]
 [[Category: Thermotoga maritima]]
-[[Category: Karakas, E.]]
+[[Category: Karakas E]]
-[[Category: Kisker, C.]]
+[[Category: Kisker C]]
-[[Category: Truglio, J J.]]
+[[Category: Truglio JJ]]
-[[Category: Endonuclase]]
-[[Category: Ner]]
-[[Category: Uvrc]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:31:31 2008''