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| ==Structure of a guideRNA-binding protein complex bound to a gRNA== | | ==Structure of a guideRNA-binding protein complex bound to a gRNA== |
- | <StructureSection load='2gje' size='340' side='right' caption='[[2gje]], [[Resolution|resolution]] 3.37Å' scene=''> | + | <StructureSection load='2gje' size='340' side='right'caption='[[2gje]], [[Resolution|resolution]] 3.37Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2gje]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Tryb2 Tryb2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GJE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GJE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2gje]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei_TREU927 Trypanosoma brucei brucei TREU927]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GJE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GJE FirstGlance]. <br> |
- | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 3.37Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gia|2gia]], [[2gid|2gid]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mrp1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=185431 TRYB2]), mrp2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=185431 TRYB2])</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=2gje FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gje OCA], [https://pdbe.org/2gje PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gje RCSB], [https://www.ebi.ac.uk/pdbsum/2gje PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gje 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=2gje FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gje OCA], [http://pdbe.org/2gje PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gje RCSB], [http://www.ebi.ac.uk/pdbsum/2gje PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2gje ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Tryb2]] | + | [[Category: Large Structures]] |
- | [[Category: Karamooz, E]] | + | [[Category: Trypanosoma brucei brucei TREU927]] |
- | [[Category: Lukes, J]] | + | [[Category: Karamooz E]] |
- | [[Category: Schumacher, M A]] | + | [[Category: Lukes J]] |
- | [[Category: Trantirek, L]] | + | [[Category: Schumacher MA]] |
- | [[Category: Zikova, A]] | + | [[Category: Trantirek L]] |
- | [[Category: Guide rna]]
| + | [[Category: Zikova A]] |
- | [[Category: Krna editing]]
| + | |
- | [[Category: Rna binding protein]]
| + | |
- | [[Category: Translation-rna complex]]
| + | |
| Structural highlights
Publication Abstract from PubMed
The mitochondrial RNA binding proteins MRP1 and MRP2 form a heteromeric complex that functions in kinetoplastid RNA editing. In this process, MRP1/MRP2 serves as a matchmaker by binding to guide RNAs and facilitating their hybridization with cognate preedited mRNAs. To understand the mechanism by which this complex performs RNA matchmaking, we determined structures of Trypanosoma brucei apoMRP1/MRP2 and an MRP1/MRP2-gRNA complex. The structures show that MRP1/MRP2 is a heterotetramer and, despite little sequence homology, each MRP subunit exhibits the same "Whirly" transcription-factor fold. The gRNA molecule binds to the highly basic beta sheet surface of the MRP complex via nonspecific, electrostatic contacts. Strikingly, while the gRNA stem/loop II base is anchored to the basic surface, stem/loop I (the anchor sequence) is unfolded and its bases exposed to solvent. Thus, MRP1/MRP2 acts as an RNA matchmaker by stabilizing the RNA molecule in an unfolded conformation suitable for RNA-RNA hybridization.
Crystal structures of T. brucei MRP1/MRP2 guide-RNA binding complex reveal RNA matchmaking mechanism.,Schumacher MA, Karamooz E, Zikova A, Trantirek L, Lukes J Cell. 2006 Aug 25;126(4):701-11. PMID:16923390[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schumacher MA, Karamooz E, Zikova A, Trantirek L, Lukes J. Crystal structures of T. brucei MRP1/MRP2 guide-RNA binding complex reveal RNA matchmaking mechanism. Cell. 2006 Aug 25;126(4):701-11. PMID:16923390 doi:S0092-8674(06)00964-0
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