3i61: Difference between revisions

Revision as of 22:51, 25 December 2014

Structure of Mss116p bound to ssRNA and ADP-Beryllium Fluoride

Structural highlights

3i61 is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	ADP, BEF, MG
Related:	3i5x, 3i5y, 3i62
Gene:	MSS116, YD9346.05C, YDR194C (Saccharomyces cerevisiae)
Resources:	FirstGlance, OCA, RCSB, PDBsum

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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The yeast DEAD box protein Mss116p is a general RNA chaperone that functions in mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Here we determined high-resolution X-ray crystal structures of Mss116p complexed with an RNA oligonucleotide and ATP analogs AMP-PNP, ADP-BeF(3)(-), or ADP-AlF(4)(-). The structures show the entire helicase core acting together with a functionally important C-terminal extension. In all structures, the helicase core is in a closed conformation with a wedge alpha helix bending RNA 3' of the central bound nucleotides, as in previous DEAD box protein structures. Notably, Mss116p's C-terminal extension also bends RNA 5' of the central nucleotides, resulting in RNA crimping. Despite reported functional differences, we observe few structural changes in ternary complexes with different ATP analogs. The structures constrain models of DEAD box protein function and reveal a strand separation mechanism in which a protein uses two wedges to act as a molecular crimper.

Structure of the Yeast DEAD box protein Mss116p reveals two wedges that crimp RNA.,Del Campo M, Lambowitz AM Mol Cell. 2009 Sep 11;35(5):598-609. PMID:19748356^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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:https://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:https://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:https://dx.doi.org/10.1073/pnas.0407896101
↑ Del Campo M, Lambowitz AM. Structure of the Yeast DEAD box protein Mss116p reveals two wedges that crimp RNA. Mol Cell. 2009 Sep 11;35(5):598-609. PMID:19748356 doi:10.1016/j.molcel.2009.07.032

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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:https://dx.doi.org/10.1038/337084a0

[2] 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

[3] 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:https://dx.doi.org/10.1002/yea.906

[4] 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:https://dx.doi.org/10.1073/pnas.0407896101

[5] Del Campo M, Lambowitz AM. Structure of the Yeast DEAD box protein Mss116p reveals two wedges that crimp RNA. Mol Cell. 2009 Sep 11;35(5):598-609. PMID:19748356 doi:10.1016/j.molcel.2009.07.032

[1]

[2]

[3]

[4]

[5]

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[3i61]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I61 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3I61 FirstGlance]. <br>
-</td></tr><tr><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><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>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3i5x|3i5x]], [[3i5y|3i5y]], [[3i62|3i62]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3i5x|3i5x]], [[3i5y|3i5y]], [[3i62|3i62]]</td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MSS116, YD9346.05C, YDR194C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MSS116, YD9346.05C, YDR194C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3i61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i61 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3i61 RCSB], [http://www.ebi.ac.uk/pdbsum/3i61 PDBsum]</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=3i61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i61 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3i61 RCSB], [http://www.ebi.ac.uk/pdbsum/3i61 PDBsum]</span></td></tr>
-<table>
+</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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 36: @@
 </StructureSection>
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Campo, M Del.]]
+[[Category: Campo, M Del]]
-[[Category: Lambowitz, A M.]]
+[[Category: Lambowitz, A M]]
 [[Category: Atp-binding]]
 [[Category: Dead-box]]

3i61: Difference between revisions

Revision as of 22:51, 25 December 2014

Structure of Mss116p bound to ssRNA and ADP-Beryllium Fluoride

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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