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2c5u
From Proteopedia
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| - | [[Image:2c5u.gif|left|200px]]<br /> | ||
| - | <applet load="2c5u" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2c5u, resolution 2.21Å" /> | ||
| - | '''T4 RNA LIGASE (RNL1) CRYSTAL STRUCTURE'''<br /> | ||
| - | == | + | ==T4 RNA Ligase (Rnl1) Crystal Structure== |
| - | + | <StructureSection load='2c5u' size='340' side='right'caption='[[2c5u]], [[Resolution|resolution]] 2.21Å' scene=''> | |
| - | [ | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[2c5u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C5U 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]] 2.21Å</td></tr> | |
| - | [ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=2c5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c5u OCA], [https://pdbe.org/2c5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c5u RCSB], [https://www.ebi.ac.uk/pdbsum/2c5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c5u ProSAT]</span></td></tr> |
| - | [[ | + | </table> |
| - | + | == Function == | |
| - | [ | + | [https://www.uniprot.org/uniprot/RLIG_BPT4 RLIG_BPT4] Involved in countering a host defense mechanism which activates T4-induced anticodon nuclease and shuts off viral translation. Repairs 5'-PO4 and 3'-OH groups in tRNA(Lys).<ref>PMID:2444436</ref> |
| - | [[ | + | == 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/c5/2c5u_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=2c5u ConSurf]. | |
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | RNA ligase type 1 from bacteriophage T4 (Rnl1) is involved in countering a host defense mechanism by repairing 5'-PO4 and 3'-OH groups in tRNA(Lys). Rnl1 is widely used as a reagent in molecular biology. Although many structures for DNA ligases are available, only fragments of RNA ligases such as Rnl2 are known. We report the first crystal structure of a complete RNA ligase, Rnl1, in complex with adenosine 5'-(alpha,beta-methylenetriphosphate) (AMPcPP). The N-terminal domain is related to the equivalent region of DNA ligases and Rnl2 and binds AMPcPP but with further interactions from the additional N-terminal 70 amino acids in Rnl1 (via Tyr37 and Arg54) and the C-terminal domain (Gly269 and Asp272). The active site contains two metal ions, consistent with the two-magnesium ion catalytic mechanism. The C-terminal domain represents a new all alpha-helical fold and has a charge distribution and architecture for helix-nucleic acid groove interaction compatible with tRNA binding. | ||
| - | + | Molecular architecture and ligand recognition determinants for T4 RNA ligase.,El Omari K, Ren J, Bird LE, Bona MK, Klarmann G, LeGrice SF, Stammers DK J Biol Chem. 2006 Jan 20;281(3):1573-9. Epub 2005 Nov 1. PMID:16263720<ref>PMID:16263720</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2c5u" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[RNA ligase|RNA ligase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia virus T4]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bird LE]] | ||
| + | [[Category: Bona MK]] | ||
| + | [[Category: El Omari K]] | ||
| + | [[Category: Klarmann G]] | ||
| + | [[Category: LeGrice SFJ]] | ||
| + | [[Category: Ren J]] | ||
| + | [[Category: Stammers DK]] | ||
Current revision
T4 RNA Ligase (Rnl1) Crystal Structure
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