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| | <StructureSection load='3rfh' size='340' side='right'caption='[[3rfh]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='3rfh' size='340' side='right'caption='[[3rfh]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3rfh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RFH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3rfh]] is a 4 chain structure with sequence from [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=3RFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RFH FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3rfg|3rfg]], [[3frx|3frx]], [[3dm0|3dm0]], [[1trj|1trj]]</div></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]] 2.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ASC1, CPC2, YM9718.15C, YMR116C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=3rfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rfh OCA], [https://pdbe.org/3rfh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rfh RCSB], [https://www.ebi.ac.uk/pdbsum/3rfh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rfh 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=3rfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rfh OCA], [https://pdbe.org/3rfh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rfh RCSB], [https://www.ebi.ac.uk/pdbsum/3rfh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rfh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/GBLP_YEAST GBLP_YEAST]] Located at the head of the 40S ribosomal subunit in the vicinity of the mRNA exit channel, it serves as a scaffold protein that can recruit other proteins to the ribosome. Involved in the negative regulation of translation of a specific subset of proteins.<ref>PMID:15340087</ref>
| + | [https://www.uniprot.org/uniprot/GBLP_YEAST GBLP_YEAST] Located at the head of the 40S ribosomal subunit in the vicinity of the mRNA exit channel, it serves as a scaffold protein that can recruit other proteins to the ribosome. Involved in the negative regulation of translation of a specific subset of proteins.<ref>PMID:15340087</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: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hein, K L]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Nilsson, J]] | + | [[Category: Hein KL]] |
| - | [[Category: Nissen, P]] | + | [[Category: Nilsson J]] |
| - | [[Category: Yatime, L]] | + | [[Category: Nissen P]] |
| - | [[Category: Beta-propeller]]
| + | [[Category: Yatime L]] |
| - | [[Category: Dimer]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
GBLP_YEAST Located at the head of the 40S ribosomal subunit in the vicinity of the mRNA exit channel, it serves as a scaffold protein that can recruit other proteins to the ribosome. Involved in the negative regulation of translation of a specific subset of proteins.[1]
Publication Abstract from PubMed
Receptor for activated C-kinase 1 (RACK1) serves as a scaffolding protein in numerous signaling pathways involving kinases and membrane-bound receptors from different cellular compartments. It exists simultaneously as a cytosolic free form and as a ribosome-bound protein. As part of the 40S ribosomal subunit, it triggers translational regulation by establishing a direct link between protein kinase C and the protein synthesis machinery. It has been suggested that RACK1 could recruit other signaling molecules onto the ribosome, providing a signal-specific modulation of the translational process. RACK1 is able to dimerize both in vitro and in vivo. This homodimer formation has been observed in several processes including the regulation of the N-methyl-d-aspartate receptor by the Fyn kinase in the brain and the oxygen-independent degradation of hypoxia-inducible factor 1. The functional relevance of this dimerization is, however, still unclear and the question of a possible dimerization of the ribosome-bound protein is still pending. Here, we report the first structure of a RACK1 homodimer, as determined from two independent crystal forms of the Saccharomyces cerevisiae RACK1 protein (also known as Asc1p) at 2.9 and 3.9 A resolution. The structure reveals an atypical mode of dimerization where monomers intertwine on blade 4, thus exposing a novel surface of the protein to potential interacting partners. We discuss the significance of the dimer structure for RACK1 function.
Structure of the RACK1 dimer from Saccharomyces cerevisiae.,Yatime L, Hein KL, Nilsson J, Nissen P J Mol Biol. 2011 Aug 12;411(2):486-98. Epub 2011 Jun 17. PMID:21704636[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gerbasi VR, Weaver CM, Hill S, Friedman DB, Link AJ. Yeast Asc1p and mammalian RACK1 are functionally orthologous core 40S ribosomal proteins that repress gene expression. Mol Cell Biol. 2004 Sep;24(18):8276-87. PMID:15340087 doi:10.1128/MCB.24.18.8276-8287.2004
- ↑ Yatime L, Hein KL, Nilsson J, Nissen P. Structure of the RACK1 dimer from Saccharomyces cerevisiae. J Mol Biol. 2011 Aug 12;411(2):486-98. Epub 2011 Jun 17. PMID:21704636 doi:10.1016/j.jmb.2011.06.017
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