5z39
From Proteopedia
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<StructureSection load='5z39' size='340' side='right' caption='[[5z39]], [[Resolution|resolution]] 2.74Å' scene=''> | <StructureSection load='5z39' size='340' side='right' caption='[[5z39]], [[Resolution|resolution]] 2.74Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5z39]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z39 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Z39 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5z39]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Dicdi Dicdi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z39 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Z39 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LHG:1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE'>LHG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEF:DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE'>PEF</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LHG:1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE'>LHG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEF:DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE'>PEF</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDB0216772 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 DICDI])</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=5z39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z39 OCA], [http://pdbe.org/5z39 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z39 RCSB], [http://www.ebi.ac.uk/pdbsum/5z39 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z39 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=5z39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z39 OCA], [http://pdbe.org/5z39 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z39 RCSB], [http://www.ebi.ac.uk/pdbsum/5z39 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z39 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | G protein interacting protein 1 (Gip1) binds and sequesters heterotrimeric G proteins in the cytosolic pool, thus regulating G protein-coupled receptor (GPCR) signalling for eukaryotic chemotaxis. Here, we report the underlying structural basis of Gip1 function. The crystal structure reveals that the region of Gip1 that binds to the G protein has a cylinder-like fold with a central hydrophobic cavity composed of six alpha-helices. Mutagenesis and biochemical analyses indicate that the hydrophobic cavity and the hydrogen bond network at the entrance of the cavity are essential for complex formation with the geranylgeranyl modification on the Ggamma subunit. Mutations of the cavity impair G protein sequestration and translocation to the membrane from the cytosol upon receptor stimulation, leading to defects in chemotaxis at higher chemoattractant concentrations. These results demonstrate that the Gip1-dependent regulation of G protein shuttling ensures wide-range gradient sensing in eukaryotic chemotaxis. | ||
| + | |||
| + | Structural basis of Gip1 for cytosolic sequestration of G protein in wide-range chemotaxis.,Miyagawa T, Koteishi H, Kamimura Y, Miyanaga Y, Takeshita K, Nakagawa A, Ueda M Nat Commun. 2018 Nov 6;9(1):4635. doi: 10.1038/s41467-018-07035-x. PMID:30401901<ref>PMID:30401901</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5z39" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Dicdi]] | ||
[[Category: Kamimura, Y]] | [[Category: Kamimura, Y]] | ||
[[Category: Koteishi, H]] | [[Category: Koteishi, H]] | ||
Revision as of 20:50, 2 December 2018
Crystal structure of C terminal region of G-protein interacting protein 1 (Gip1) from Dictyostelium discoideum form II
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