5ivl: Difference between revisions
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==CshA Helicase== | ==CshA Helicase== | ||
<StructureSection load='5ivl' size='340' side='right' caption='[[5ivl]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='5ivl' size='340' side='right'caption='[[5ivl]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ivl]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5ivl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus_10 Geobacillus stearothermophilus 10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IVL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IVL FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ivl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ivl OCA], [https://pdbe.org/5ivl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ivl RCSB], [https://www.ebi.ac.uk/pdbsum/5ivl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ivl ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5ivl" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5ivl" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Helicase 3D structures|Helicase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Geobacillus stearothermophilus 10]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Huen | [[Category: Huen J]] | ||
[[Category: Li | [[Category: Li C-L]] | ||
[[Category: Lin | [[Category: Lin C-L]] | ||
[[Category: Yi | [[Category: Yi W-L]] | ||
[[Category: Yuan | [[Category: Yuan H]] | ||
Latest revision as of 13:33, 6 September 2023
CshA HelicaseCshA Helicase
Structural highlights
Publication Abstract from PubMedCshA is a dimeric DEAD-box helicase that cooperates with ribonucleases for mRNA turnover. The molecular mechanism for how a dimeric DEAD-box helicase aids in RNA decay remains unknown. Here, we report the crystal structure and small-angle X-ray scattering solution structure of the CshA from Geobacillus stearothermophilus. In contrast to typical monomeric DEAD-box helicases, CshA is exclusively a dimeric protein with the RecA-like domains of each protomer forming a V-shaped structure. We show that the C-terminal domains protruding outward from the tip of the V-shaped structure is critical for mediating strong RNA binding and is crucial for efficient RNA-dependent ATP hydrolysis. We also show that RNA remains bound with CshA during ATP hydrolysis cycles and thus bulk RNAs could be unwound and degraded in a processive manner through cooperation between exoribonucleases and CshA. A dimeric helicase is hence preserved in RNA-degrading machinery for efficient RNA turnover in prokaryotes and eukaryotes. Structural Insights into a Unique Dimeric DEAD-Box Helicase CshA that Promotes RNA Decay.,Huen J, Lin CL, Golzarroshan B, Yi WL, Yang WZ, Yuan HS Structure. 2017 Mar 7;25(3):469-481. doi: 10.1016/j.str.2017.01.012. Epub 2017, Feb 23. PMID:28238534[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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