4o1o: Difference between revisions
New page: '''Unreleased structure''' The entry 4o1o is ON HOLD Authors: Huang, H., Zeqiraj, E, Ceccarelli, D.F., Sicheri, F. Description: Crystal Structure of RNase L in complex with 2-5A |
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==Crystal Structure of RNase L in complex with 2-5A== | |||
<StructureSection load='4o1o' size='340' side='right'caption='[[4o1o]], [[Resolution|resolution]] 3.27Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4o1o]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O1O 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]] 3.27Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=25L:[[(2R,3R,4R,5R)-5-(6-AMINOPURIN-9-YL)-4-[[(2R,3R,4R,5R)-5-(6-AMINOPURIN-9-YL)-4-[[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHOXY-HYDROXY-PHOSPHORYL]OXY-3-HYDROXY-OXOLAN-2-YL]METHOXY-HYDROXY-PHOSPHORYL]OXY-3-HYDROXY-OXOLAN-2-YL]METHOXY-HYDROXY-PHOSPHORYL]+PHOSPHONO+HYDROGEN+PHOSPHATE'>25L</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=4o1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o1o OCA], [https://pdbe.org/4o1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o1o RCSB], [https://www.ebi.ac.uk/pdbsum/4o1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o1o ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A5H025_PIG A5H025_PIG] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
RNase L is an ankyrin repeat domain-containing dual endoribonuclease-pseudokinase that is activated by unusual 2,'5'-oligoadenylate (2-5A) second messengers and which impedes viral infections in higher vertebrates. Despite its importance in interferon-regulated antiviral innate immunity, relatively little is known about its precise mechanism of action. Here we present a functional characterization of 2.5 A and 3.25 A X-ray crystal and small-angle X-ray scattering structures of RNase L bound to a natural 2-5A activator with and without ADP or the nonhydrolysable ATP mimetic AMP-PNP. These studies reveal how recognition of 2-5A through interactions with the ankyrin repeat domain and the pseudokinase domain, together with nucleotide binding, imposes a rigid intertwined dimer configuration that is essential for RNase catalytic and antiviral functions. The involvement of the pseudokinase domain of RNase L in 2-5A sensing, nucleotide binding, dimerization, and ribonuclease functions highlights the evolutionary adaptability of the eukaryotic protein kinase fold. | |||
Dimeric structure of pseudokinase RNase L bound to 2-5A reveals a basis for interferon-induced antiviral activity.,Huang H, Zeqiraj E, Dong B, Jha BK, Duffy NM, Orlicky S, Thevakumaran N, Talukdar M, Pillon MC, Ceccarelli DF, Wan LC, Juang YC, Mao DY, Gaughan C, Brinton MA, Perelygin AA, Kourinov I, Guarne A, Silverman RH, Sicheri F Mol Cell. 2014 Jan 23;53(2):221-34. doi: 10.1016/j.molcel.2013.12.025. PMID:24462203<ref>PMID:24462203</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4o1o" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Sus scrofa]] | |||
[[Category: Ceccarelli DF]] | |||
[[Category: Huang H]] | |||
[[Category: Sicheri F]] | |||
[[Category: Zeqiraj E]] | |||
Latest revision as of 20:05, 20 September 2023
Crystal Structure of RNase L in complex with 2-5ACrystal Structure of RNase L in complex with 2-5A
Structural highlights
FunctionPublication Abstract from PubMedRNase L is an ankyrin repeat domain-containing dual endoribonuclease-pseudokinase that is activated by unusual 2,'5'-oligoadenylate (2-5A) second messengers and which impedes viral infections in higher vertebrates. Despite its importance in interferon-regulated antiviral innate immunity, relatively little is known about its precise mechanism of action. Here we present a functional characterization of 2.5 A and 3.25 A X-ray crystal and small-angle X-ray scattering structures of RNase L bound to a natural 2-5A activator with and without ADP or the nonhydrolysable ATP mimetic AMP-PNP. These studies reveal how recognition of 2-5A through interactions with the ankyrin repeat domain and the pseudokinase domain, together with nucleotide binding, imposes a rigid intertwined dimer configuration that is essential for RNase catalytic and antiviral functions. The involvement of the pseudokinase domain of RNase L in 2-5A sensing, nucleotide binding, dimerization, and ribonuclease functions highlights the evolutionary adaptability of the eukaryotic protein kinase fold. Dimeric structure of pseudokinase RNase L bound to 2-5A reveals a basis for interferon-induced antiviral activity.,Huang H, Zeqiraj E, Dong B, Jha BK, Duffy NM, Orlicky S, Thevakumaran N, Talukdar M, Pillon MC, Ceccarelli DF, Wan LC, Juang YC, Mao DY, Gaughan C, Brinton MA, Perelygin AA, Kourinov I, Guarne A, Silverman RH, Sicheri F Mol Cell. 2014 Jan 23;53(2):221-34. doi: 10.1016/j.molcel.2013.12.025. PMID:24462203[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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