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| | <StructureSection load='5wds' size='340' side='right'caption='[[5wds]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='5wds' size='340' side='right'caption='[[5wds]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5wds]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Choanoflagellata Choanoflagellata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WDS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WDS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5wds]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Choanoflagellata Choanoflagellata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WDS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WDS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.85Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTSG_05504 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28009 Choanoflagellata])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Small_monomeric_GTPase Small monomeric GTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.2 3.6.5.2] </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=5wds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wds OCA], [https://pdbe.org/5wds PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wds RCSB], [https://www.ebi.ac.uk/pdbsum/5wds PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wds 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=5wds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wds OCA], [http://pdbe.org/5wds PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wds RCSB], [http://www.ebi.ac.uk/pdbsum/5wds PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wds ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/F2UBE5_SALR5 F2UBE5_SALR5] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Choanoflagellata]] | | [[Category: Choanoflagellata]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Small monomeric GTPase]]
| + | [[Category: Gee CL]] |
| - | [[Category: Gee, C L]] | + | [[Category: Kondo Y]] |
| - | [[Category: Kondo, Y]] | + | [[Category: Kuriyan J]] |
| - | [[Category: Kuriyan, J]] | + | |
| - | [[Category: Gtpase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Oncoprotein]]
| + | |
| - | [[Category: Small g-protein]]
| + | |
| Structural highlights
Function
F2UBE5_SALR5
Publication Abstract from PubMed
Ras proteins are highly conserved signaling molecules that exhibit regulated, nucleotide-dependent switching between active and inactive states. The high conservation of Ras requires mechanistic explanation, especially given the general mutational tolerance of proteins. Here, we use deep mutational scanning, biochemical analysis and molecular simulations to understand constraints on Ras sequence. Ras exhibits global sensitivity to mutation when regulated by a GTPase activating protein and a nucleotide exchange factor. Removing the regulators shifts the distribution of mutational effects to be largely neutral, and reveals hotspots of activating mutations in residues that restrain Ras dynamics and promote the inactive state. Evolutionary analysis, combined with structural and mutational data, argue that Ras has co-evolved with its regulators in the vertebrate lineage. Overall, our results show that sequence conservation in Ras depends strongly on the biochemical network in which it operates, providing a framework for understanding the origin of global selection pressures on proteins.
Deconstruction of the Ras switching cycle through saturation mutagenesis.,Bandaru P, Shah NH, Bhattacharyya M, Barton JP, Kondo Y, Cofsky JC, Gee CL, Chakraborty AK, Kortemme T, Ranganathan R, Kuriyan J Elife. 2017 Jul 7;6. pii: e27810. doi: 10.7554/eLife.27810. PMID:28686159[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bandaru P, Shah NH, Bhattacharyya M, Barton JP, Kondo Y, Cofsky JC, Gee CL, Chakraborty AK, Kortemme T, Ranganathan R, Kuriyan J. Deconstruction of the Ras switching cycle through saturation mutagenesis. Elife. 2017 Jul 7;6. pii: e27810. doi: 10.7554/eLife.27810. PMID:28686159 doi:http://dx.doi.org/10.7554/eLife.27810
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