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| | ==Structure of Rbg1 in complex with Tma46 dfrp domain== | | ==Structure of Rbg1 in complex with Tma46 dfrp domain== |
| - | <StructureSection load='4a9a' size='340' side='right' caption='[[4a9a]], [[Resolution|resolution]] 2.67Å' scene=''> | + | <StructureSection load='4a9a' size='340' side='right'caption='[[4a9a]], [[Resolution|resolution]] 2.67Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4a9a]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A9A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A9A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4a9a]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A9A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A9A FirstGlance]. <br> |
| - | </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=4a9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a9a OCA], [http://pdbe.org/4a9a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a9a RCSB], [http://www.ebi.ac.uk/pdbsum/4a9a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a9a ProSAT]</span></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]] 2.67Å</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=4a9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a9a OCA], [https://pdbe.org/4a9a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a9a RCSB], [https://www.ebi.ac.uk/pdbsum/4a9a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a9a ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RBG1_YEAST RBG1_YEAST]] Involved in ribosomal function.<ref>PMID:19448108</ref> | + | [https://www.uniprot.org/uniprot/RBG1_YEAST RBG1_YEAST] Involved in ribosomal function.<ref>PMID:19448108</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | + | [[Category: Large Structures]] |
| - | [[Category: Bravo, J]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Daugeron, M]] | + | [[Category: Bravo J]] |
| - | [[Category: Francis, S M]] | + | [[Category: Daugeron M]] |
| - | [[Category: Gas, M]] | + | [[Category: Francis SM]] |
| - | [[Category: Seraphin, B]] | + | [[Category: Gas M]] |
| - | [[Category: Drg-dfrp complex]]
| + | [[Category: Seraphin B]] |
| - | [[Category: Ribosome binding gtpase]]
| + | |
| - | [[Category: Translation]]
| + | |
| Structural highlights
Function
RBG1_YEAST Involved in ribosomal function.[1]
Publication Abstract from PubMed
Developmentally Regulated GTP-binding (DRG) proteins are highly conserved GTPases that associate with DRG Family Regulatory Proteins (DFRP). The resulting complexes have recently been shown to participate in eukaryotic translation. The structure of the Rbg1 GTPase, a yeast DRG protein, in complex with the C-terminal region of its DFRP partner, Tma46, was solved by X-ray diffraction. These data reveal that DRG proteins are multimodular factors with three additional domains, helix-turn-helix (HTH), S5D2L and TGS, packing against the GTPase platform. Surprisingly, the S5D2L domain is inserted in the middle of the GTPase sequence. In contrast, the region of Tma46 interacting with Rbg1 adopts an extended conformation typical of intrinsically unstructured proteins and contacts the GTPase and TGS domains. Functional analyses demonstrate that the various domains of Rbg1, as well as Tma46, modulate the GTPase activity of Rbg1 and contribute to the function of these proteins in vivo. Dissecting the role of the different domains revealed that the Rbg1 TGS domain is essential for the recruitment of this factor in polysomes, supporting further the implication of these conserved factors in translation.
Rbg1-Tma46 dimer structure reveals new functional domains and their role in polysome recruitment.,Francis SM, Gas ME, Daugeron MC, Bravo J, Seraphin B Nucleic Acids Res. 2012 Sep 23. PMID:23002146[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wout PK, Sattlegger E, Sullivan SM, Maddock JR. Saccharomyces cerevisiae Rbg1 protein and its binding partner Gir2 interact on Polyribosomes with Gcn1. Eukaryot Cell. 2009 Jul;8(7):1061-71. Epub 2009 May 15. PMID:19448108 doi:http://dx.doi.org/EC.00356-08
- ↑ Francis SM, Gas ME, Daugeron MC, Bravo J, Seraphin B. Rbg1-Tma46 dimer structure reveals new functional domains and their role in polysome recruitment. Nucleic Acids Res. 2012 Sep 23. PMID:23002146 doi:http://dx.doi.org/10.1093/nar/gks867
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