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| | ==DEAD-box helicase Mss116 bound to ssDNA and ADP-BeF== | | ==DEAD-box helicase Mss116 bound to ssDNA and ADP-BeF== |
| - | <StructureSection load='4tyn' size='340' side='right' caption='[[4tyn]], [[Resolution|resolution]] 2.96Å' scene=''> | + | <StructureSection load='4tyn' size='340' side='right'caption='[[4tyn]], [[Resolution|resolution]] 2.96Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4tyn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TYN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TYN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4tyn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TYN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.959Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4tyw|4tyw]], [[4tyy|4tyy]], [[4tz0|4tz0]], [[4tz6|4tz6]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=4tyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tyn OCA], [https://pdbe.org/4tyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tyn RCSB], [https://www.ebi.ac.uk/pdbsum/4tyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tyn 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=4tyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tyn OCA], [http://pdbe.org/4tyn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tyn RCSB], [http://www.ebi.ac.uk/pdbsum/4tyn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tyn ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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> | + | [https://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Helicase|Helicase]] | + | *[[Helicase 3D structures|Helicase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: RNA helicase]] | + | [[Category: Large Structures]] |
| - | [[Category: Lambowitz, A M]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Mallam, A L]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Sidote, D J]] | + | [[Category: Lambowitz AM]] |
| - | [[Category: Dead-box]] | + | [[Category: Mallam AL]] |
| - | [[Category: Hydrolase]] | + | [[Category: Sidote DJ]] |
| - | [[Category: Hydrolase-dna complex]]
| + | |
| - | [[Category: Rna binding protein-dna complex]]
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| - | [[Category: Rna helicase]]
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| 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 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[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Seraphin B, Simon M, Boulet A, Faye G. Mitochondrial splicing requires a protein from a novel helicase family. Nature. 1989 Jan 5;337(6202):84-7. PMID:2535893 doi:http://dx.doi.org/10.1038/337084a0
- ↑ Niemer I, Schmelzer C, Borner GV. Overexpression of DEAD box protein pMSS116 promotes ATP-dependent splicing of a yeast group II intron in vitro. Nucleic Acids Res. 1995 Sep 11;23(17):2966-72. PMID:7567443
- ↑ Minczuk M, Dmochowska A, Palczewska M, Stepien PP. Overexpressed yeast mitochondrial putative RNA helicase Mss116 partially restores proper mtRNA metabolism in strains lacking the Suv3 mtRNA helicase. Yeast. 2002 Nov;19(15):1285-93. PMID:12402239 doi:http://dx.doi.org/10.1002/yea.906
- ↑ Huang HR, Rowe CE, Mohr S, Jiang Y, Lambowitz AM, Perlman PS. The splicing of yeast mitochondrial group I and group II introns requires a DEAD-box protein with RNA chaperone function. Proc Natl Acad Sci U S A. 2005 Jan 4;102(1):163-8. Epub 2004 Dec 23. PMID:15618406 doi:http://dx.doi.org/10.1073/pnas.0407896101
- ↑ Mallam AL, Sidote DJ, Lambowitz AM. Molecular insights into RNA and DNA helicase evolution from the determinants of specificity for a DEAD-box RNA helicase. Elife. 2014 Dec 12;3. doi: 10.7554/eLife.04630. PMID:25497230 doi:http://dx.doi.org/10.7554/eLife.04630
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