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| | <StructureSection load='5i8q' size='340' side='right'caption='[[5i8q]], [[Resolution|resolution]] 4.20Å' scene=''> | | <StructureSection load='5i8q' size='340' side='right'caption='[[5i8q]], [[Resolution|resolution]] 4.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5i8q]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [http://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=5I8Q OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5I8Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5i8q]] is a 4 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=5I8Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5I8Q FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</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]] 4.2Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5i8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i8q OCA], [http://pdbe.org/5i8q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i8q RCSB], [http://www.ebi.ac.uk/pdbsum/5i8q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5i8q ProSAT]</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=5i8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i8q OCA], [https://pdbe.org/5i8q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5i8q RCSB], [https://www.ebi.ac.uk/pdbsum/5i8q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5i8q ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PRP43_YEAST PRP43_YEAST]] Pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA.<ref>PMID:9342317</ref> <ref>PMID:16880513</ref> | + | [https://www.uniprot.org/uniprot/PRP43_YEAST PRP43_YEAST] Pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA.<ref>PMID:9342317</ref> <ref>PMID:16880513</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 3D structures|Helicase 3D structures]] | | *[[Helicase 3D structures|Helicase 3D structures]] |
| | + | *[[Pre-mRNA splicing factors 3D structures|Pre-mRNA splicing factors 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: RNA helicase]] | |
| | [[Category: Saccharomyces cerevisiae]] | | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Saccharomyces cerevisiae s288c]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Andersen, G R]] | + | [[Category: Andersen GR]] |
| - | [[Category: He, Y]] | + | [[Category: He Y]] |
| - | [[Category: Nielsen, K H]] | + | [[Category: Nielsen KH]] |
| - | [[Category: Helicase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Rna]]
| + | |
| - | [[Category: Unwinding]]
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| Structural highlights
Function
PRP43_YEAST Pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA.[1] [2]
Publication Abstract from PubMed
Three families of nucleic acid-dependent ATPases (DEAH/RHA, Ski2-like, and NS3/NPH-II), termed the DExH ATPases, are thought to execute myriad functions by processive, ATP-dependent, 3' to 5' translocation along single-stranded nucleic acid. While the mechanism of translocation of the viral NS3/NPH-II family has been studied extensively, it has not been clear if or how the principles that have emerged for this family extend to the other two families. Here we report the crystal structure of the yeast DEAH/RHA family ATPase Prp43p, which functions in splicing and ribosome biogenesis, in complex with poly-uracil and a nonhydrolyzable ATP analog. The structure reveals a conserved DEAH/RHA-specific variation of motif Ib within the RecA1 domain of the catalytic core, in which the motif elongates as a beta-hairpin that bookends the 3' end of a central RNA stack, a function that in the viral and Ski-2 families is performed by an auxiliary domain. Supporting a fundamental role in translocation, mutations in this hairpin abolished helicase activity without affecting RNA binding or ATPase activity. While the structure reveals differences with viral ATPases in the RecA1 domain, our structure demonstrates striking similarities with viral ATPases in the RecA2 domain of the catalytic core, including both a prominent beta-hairpin that bookends the 5' end of the RNA stack and a dynamic motif Va that is implicated in mediating translocation. Our crystal structure, genetic, and biochemical experiments, as well as comparisons with other DExH ATPases, support a generalized mechanism for the DExH class of helicases involving a pair of bookends that inchworm along RNA.
Structure of the DEAH/RHA ATPase Prp43p bound to RNA implicates a pair of hairpins and motif Va in translocation along RNA.,He Y, Staley JP, Andersen GR, Nielsen KH RNA. 2017 Jul;23(7):1110-1124. doi: 10.1261/rna.060954.117. Epub 2017 Apr 17. PMID:28416566[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Arenas JE, Abelson JN. Prp43: An RNA helicase-like factor involved in spliceosome disassembly. Proc Natl Acad Sci U S A. 1997 Oct 28;94(22):11798-802. PMID:9342317
- ↑ Boon KL, Auchynnikava T, Edwalds-Gilbert G, Barrass JD, Droop AP, Dez C, Beggs JD. Yeast ntr1/spp382 mediates prp43 function in postspliceosomes. Mol Cell Biol. 2006 Aug;26(16):6016-23. PMID:16880513 doi:http://dx.doi.org/10.1128/MCB.02347-05
- ↑ He Y, Staley JP, Andersen GR, Nielsen KH. Structure of the DEAH/RHA ATPase Prp43p bound to RNA implicates a pair of hairpins and motif Va in translocation along RNA. RNA. 2017 Jul;23(7):1110-1124. doi: 10.1261/rna.060954.117. Epub 2017 Apr 17. PMID:28416566 doi:http://dx.doi.org/10.1261/rna.060954.117
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