5ivl: Difference between revisions
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<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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IVL FirstGlance]. <br> | <table><tr><td colspan='2'>[[5ivl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_stearothermophilus_10 Bacillus 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IVL FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cshA, GT50_10605 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272567 Bacillus stearothermophilus 10])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA_helicase RNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.13 3.6.4.13] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA_helicase RNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.13 3.6.4.13] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ivl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ivl OCA], [http://pdbe.org/5ivl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ivl RCSB], [http://www.ebi.ac.uk/pdbsum/5ivl PDBsum], [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ivl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ivl OCA], [http://pdbe.org/5ivl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ivl RCSB], [http://www.ebi.ac.uk/pdbsum/5ivl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ivl ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/A0A0K2H973_GEOSE A0A0K2H973_GEOSE]] DEAD-box RNA helicase possibly involved in RNA degradation. Unwinds dsRNA in both 5'- and 3'-directions, has RNA-dependent ATPase activity.[HAMAP-Rule:MF_01493] | [[http://www.uniprot.org/uniprot/A0A0K2H973_GEOSE A0A0K2H973_GEOSE]] DEAD-box RNA helicase possibly involved in RNA degradation. Unwinds dsRNA in both 5'- and 3'-directions, has RNA-dependent ATPase activity.[HAMAP-Rule:MF_01493] | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
CshA 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<ref>PMID:28238534</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5ivl" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus stearothermophilus 10]] | |||
[[Category: RNA helicase]] | [[Category: RNA helicase]] | ||
[[Category: Huen, J]] | [[Category: Huen, J]] | ||
Revision as of 10:43, 8 November 2017
CshA HelicaseCshA Helicase
Structural highlights
Function[A0A0K2H973_GEOSE] DEAD-box RNA helicase possibly involved in RNA degradation. Unwinds dsRNA in both 5'- and 3'-directions, has RNA-dependent ATPase activity.[HAMAP-Rule:MF_01493] 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. References
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