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6vu8
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of G-alpha-i bound to its chaperone Ric-8A== | |
| + | <StructureSection load='6vu8' size='340' side='right'caption='[[6vu8]], [[Resolution|resolution]] 4.14Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6vu8]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VU8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6VU8 FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6vu5|6vu5]]</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=6vu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vu8 OCA], [http://pdbe.org/6vu8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vu8 RCSB], [http://www.ebi.ac.uk/pdbsum/6vu8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vu8 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/GNAI1_HUMAN GNAI1_HUMAN]] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division.<ref>PMID:17635935</ref> <ref>PMID:17264214</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Many chaperones promote nascent polypeptide folding followed by substrate release through ATP-dependent conformational changes. Here we show cryoEM structures of Galpha subunit folding intermediates in complex with full-length Ric-8A, a unique chaperone-client system in which substrate release is facilitated by guanine nucleotide binding to the client G protein. The structures of Ric-8A-Galphai and Ric-8A-Galphaq complexes reveal that the chaperone employs its extended C-terminal region to cradle the Ras-like domain of Galpha, positioning the Ras core in contact with the Ric-8A core while engaging its switch2 nucleotide binding region. The C-terminal alpha5 helix of Galpha is held away from the Ras-like domain through Ric-8A core domain interactions, which critically depend on recognition of the Galpha C terminus by the chaperone. The structures, complemented with biochemical and cellular chaperoning data, support a folding quality control mechanism that ensures proper formation of the C-terminal alpha5 helix before allowing GTP-gated release of Galpha from Ric-8A. | ||
| - | + | Structures of Galpha Proteins in Complex with Their Chaperone Reveal Quality Control Mechanisms.,Seven AB, Hilger D, Papasergi-Scott MM, Zhang L, Qu Q, Kobilka BK, Tall GG, Skiniotis G Cell Rep. 2020 Feb 28. pii: S2211-1247(20)30260-6. doi:, 10.1016/j.celrep.2020.02.086. PMID:32126208<ref>PMID:32126208</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6vu8" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Hilger, D]] | ||
| + | [[Category: Seven, A B]] | ||
| + | [[Category: Chaperone]] | ||
| + | [[Category: Cryoem structure]] | ||
| + | [[Category: G alpha folding]] | ||
| + | [[Category: G protein alpha subunit]] | ||
| + | [[Category: Molecular chaperone]] | ||
| + | [[Category: Phosphorylation]] | ||
| + | [[Category: Protein complex]] | ||
| + | [[Category: Quality control]] | ||
| + | [[Category: Ric-8]] | ||
Revision as of 10:03, 18 March 2020
Structure of G-alpha-i bound to its chaperone Ric-8A
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