1s68: Difference between revisions

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[[Image:1s68.jpg|left|200px]]


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==Structure and Mechanism of RNA Ligase==
The line below this paragraph, containing "STRUCTURE_1s68", creates the "Structure Box" on the page.
<StructureSection load='1s68' size='340' side='right'caption='[[1s68]], [[Resolution|resolution]] 1.90&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'>[[1s68]] is a 1 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=1S68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S68 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]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene></td></tr>
{{STRUCTURE_1s68| PDB=1s68 |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1s68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s68 OCA], [https://pdbe.org/1s68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s68 RCSB], [https://www.ebi.ac.uk/pdbsum/1s68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s68 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RLIG2_BPT4 RLIG2_BPT4] Catalyzes intramolecular and intermolecular RNA strand joining (in vitro). May play a role in the repair of nicked RNA molecules.<ref>PMID:12228725</ref> <ref>PMID:17018278</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/s6/1s68_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=1s68 ConSurf].
<div style="clear:both"></div>


'''Structure and Mechanism of RNA Ligase'''
==See Also==
 
*[[RNA ligase|RNA ligase]]
 
== References ==
==Overview==
<references/>
T4 RNA ligase 2 (Rnl2) exemplifies an RNA ligase family that includes the RNA editing ligases (RELs) of Trypanosoma and Leishmania. The Rnl2/REL enzymes are defined by essential signature residues and a unique C-terminal domain, which we show is essential for sealing of 3'-OH and 5'-PO4 RNA ends by Rnl2, but not for ligase adenylation or phosphodiester bond formation at a preadenylated AppRNA end. The N-terminal segment Rnl2(1-249) of the 334 aa Rnl2 protein comprises an autonomous adenylyltransferase/AppRNA ligase domain. We report the 1.9 A crystal structure of the ligase domain with AMP bound at the active site, which reveals a shared fold, catalytic mechanism, and evolutionary history for RNA ligases, DNA ligases, and mRNA capping enzymes.
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Escherichia virus T4]]
1S68 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S68 OCA].
[[Category: Large Structures]]
 
[[Category: Ho CK]]
==Reference==
[[Category: Lima CD]]
Structure and mechanism of RNA ligase., Ho CK, Wang LK, Lima CD, Shuman S, Structure. 2004 Feb;12(2):327-39. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14962393 14962393]
[[Category: Shuman S]]
[[Category: Enterobacteria phage t4]]
[[Category: Wang LK]]
[[Category: Single protein]]
[[Category: Ho, C K.]]
[[Category: Lima, C D.]]
[[Category: Shuman, S.]]
[[Category: Wang, L K.]]
[[Category: Ribonucleic acid ligase]]
[[Category: Rna repair]]
[[Category: T4]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:21:15 2008''

Latest revision as of 11:28, 14 February 2024

Structure and Mechanism of RNA LigaseStructure and Mechanism of RNA Ligase

Structural highlights

1s68 is a 1 chain structure with sequence from Escherichia virus T4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RLIG2_BPT4 Catalyzes intramolecular and intermolecular RNA strand joining (in vitro). May play a role in the repair of nicked RNA molecules.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Ho CK, Shuman S. Bacteriophage T4 RNA ligase 2 (gp24.1) exemplifies a family of RNA ligases found in all phylogenetic domains. Proc Natl Acad Sci U S A. 2002 Oct 1;99(20):12709-14. Epub 2002 Sep 12. PMID:12228725 doi:http://dx.doi.org/10.1073/pnas.192184699
  2. ↑ Nandakumar J, Shuman S, Lima CD. RNA ligase structures reveal the basis for RNA specificity and conformational changes that drive ligation forward. Cell. 2006 Oct 6;127(1):71-84. PMID:17018278 doi:10.1016/j.cell.2006.08.038

1s68, resolution 1.90Å

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