4tz6: Difference between revisions
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''' | ==DEAD-box helicase Mss116 bound to ssRNA and UDP-BeF== | ||
<StructureSection load='4tz6' size='340' side='right' caption='[[4tz6]], [[Resolution|resolution]] 3.21Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4tz6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TZ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TZ6 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4tyn|4tyn]], [[4tyw|4tyw]], [[4tyy|4tyy]], [[4tz0|4tz0]]</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=4tz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tz6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tz6 RCSB], [http://www.ebi.ac.uk/pdbsum/4tz6 PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/MS116_YEAST MS116_YEAST]] ATP-dependent RNA helicase required for mitochondrial splicing of group I and II introns. Specifically involved in the ATP-dependent splicing of the bl1 intron of COB. Also required for efficient mitochondrial translation.<ref>PMID:2535893</ref> <ref>PMID:7567443</ref> <ref>PMID:12402239</ref> <ref>PMID:15618406</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
How different helicase families with a conserved catalytic 'helicase core' evolved to function on varied RNA and DNA substrates by diverse mechanisms remains unclear. Here, we used Mss116, a yeast DEAD-box protein that utilizes ATP to locally unwind dsRNA, to investigate helicase specificity and mechanism. Our results define the molecular basis for the substrate specificity of a DEAD-box protein. Additionally, they show that Mss116 has ambiguous substrate-binding properties and interacts with all four NTPs and both RNA and DNA. The efficiency of unwinding correlates with the stability of the 'closed-state' helicase core, a complex with nucleotide and nucleic acid that forms as duplexes are unwound. Crystal structures reveal that core stability is modulated by family-specific interactions that favor certain substrates. This suggests how present-day helicases diversified from an ancestral core with broad specificity by retaining core closure as a common catalytic mechanism while optimizing substrate-binding interactions for different cellular functions. | |||
Molecular insights into RNA and DNA helicase evolution from the determinants of specificity for a DEAD-box RNA helicase.,Mallam AL, Sidote DJ, Lambowitz AM Elife. 2014 Dec 12;3. doi: 10.7554/eLife.04630. PMID:25497230<ref>PMID:25497230</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: Sidote, D | </StructureSection> | ||
[[Category: | [[Category: RNA helicase]] | ||
[[Category: Lambowitz, A M]] | |||
[[Category: Mallam, A L]] | |||
[[Category: Sidote, D J]] | |||
[[Category: Dead-box]] | |||
[[Category: Hydrolase]] | |||
[[Category: Rna binding protein-rna complex]] | |||
[[Category: Rna helicase]] | |||
Revision as of 19:35, 28 January 2015
DEAD-box helicase Mss116 bound to ssRNA and UDP-BeFDEAD-box helicase Mss116 bound to ssRNA and UDP-BeF
Structural highlights
Function[MS116_YEAST] ATP-dependent RNA helicase required for mitochondrial splicing of group I and II introns. Specifically involved in the ATP-dependent splicing of the bl1 intron of COB. Also required for efficient mitochondrial translation.[1] [2] [3] [4] Publication Abstract from PubMedHow different helicase families with a conserved catalytic 'helicase core' evolved to function on varied RNA and DNA substrates by diverse mechanisms remains unclear. Here, we used Mss116, a yeast DEAD-box protein that utilizes ATP to locally unwind dsRNA, to investigate helicase specificity and mechanism. Our results define the molecular basis for the substrate specificity of a DEAD-box protein. Additionally, they show that Mss116 has ambiguous substrate-binding properties and interacts with all four NTPs and both RNA and DNA. The efficiency of unwinding correlates with the stability of the 'closed-state' helicase core, a complex with nucleotide and nucleic acid that forms as duplexes are unwound. Crystal structures reveal that core stability is modulated by family-specific interactions that favor certain substrates. This suggests how present-day helicases diversified from an ancestral core with broad specificity by retaining core closure as a common catalytic mechanism while optimizing substrate-binding interactions for different cellular functions. Molecular insights into RNA and DNA helicase evolution from the determinants of specificity for a DEAD-box RNA helicase.,Mallam AL, Sidote DJ, Lambowitz AM Elife. 2014 Dec 12;3. doi: 10.7554/eLife.04630. PMID:25497230[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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