2fyh: Difference between revisions
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New page: left|200px<br /><applet load="2fyh" size="350" color="white" frame="true" align="right" spinBox="true" caption="2fyh" /> '''Solution structure of the 2'-5' RNA ligase-l... |
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== | ==Solution structure of the 2'-5' RNA ligase-like protein from Pyrococcus furiosus== | ||
<StructureSection load='2fyh' size='340' side='right'caption='[[2fyh]]' scene=''> | |||
[ | == Structural highlights == | ||
[[ | <table><tr><td colspan='2'>[[2fyh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus_DSM_3638 Pyrococcus furiosus DSM 3638]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FYH FirstGlance]. <br> | ||
[[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2fyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fyh OCA], [https://pdbe.org/2fyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fyh RCSB], [https://www.ebi.ac.uk/pdbsum/2fyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fyh ProSAT], [https://www.topsan.org/Proteins/RSGI/2fyh TOPSAN]</span></td></tr> | ||
</table> | |||
[ | == Function == | ||
[[ | [https://www.uniprot.org/uniprot/THPR_PYRFU THPR_PYRFU] Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester. In vitro, ligates 5' and 3' half-tRNA molecules with 2',3'-cyclic phosphate and 5'-hydroxyl termini, respectively, to the product containing the 2'-5' phosphodiester linkage. Ligase activity requires GTP, but GTP hydrolysis is not required for the reaction, which is reversible. Ligase activity is weak compared to the phosphodiesterase activity.<ref>PMID:19155324</ref> | ||
[ | == Evolutionary Conservation == | ||
[ | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | |||
[[Category: | <jmolCheckbox> | ||
[[Category: | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fy/2fyh_consurf.spt"</scriptWhenChecked> | ||
[[Category: | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
[[Category: | <text>to colour the structure by Evolutionary Conservation</text> | ||
[[Category: | </jmolCheckbox> | ||
[[Category: | </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=2fyh ConSurf]. | ||
[[Category: | <div style="clear:both"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pyrococcus furiosus DSM 3638]] | |||
[[Category: Kanai A]] | |||
[[Category: Kawai G]] | |||
[[Category: Matsuda T]] | |||
[[Category: Muto Y]] | |||
[[Category: Okada K]] | |||
[[Category: Sakamoto T]] | |||
[[Category: Yokoyama S]] | |||
Latest revision as of 09:40, 1 May 2024
Solution structure of the 2'-5' RNA ligase-like protein from Pyrococcus furiosusSolution structure of the 2'-5' RNA ligase-like protein from Pyrococcus furiosus
Structural highlights
FunctionTHPR_PYRFU Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester. In vitro, ligates 5' and 3' half-tRNA molecules with 2',3'-cyclic phosphate and 5'-hydroxyl termini, respectively, to the product containing the 2'-5' phosphodiester linkage. Ligase activity requires GTP, but GTP hydrolysis is not required for the reaction, which is reversible. Ligase activity is weak compared to the phosphodiesterase activity.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. References
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