6vu5: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

The entry ~~6vu5~~ is ~~ON HOLD until Feb 14 2022~~

==Structure of G-alpha-q bound to its chaperone Ric-8A==

== Structural highlights ==

<table><tr><td colspan='2'>[[6vu5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VU5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6VU5 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>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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=6vu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vu5 OCA], [http://pdbe.org/6vu5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vu5 RCSB], [http://www.ebi.ac.uk/pdbsum/6vu5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vu5 ProSAT]</span></td></tr>

</table>

== Disease ==

[[http://www.uniprot.org/uniprot/GNAQ_HUMAN GNAQ_HUMAN]] Sturge-Weber syndrome;Phakomatosis cesioflammea;Uveal melanoma;Familial multiple nevi flammei. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.

== Function ==

[[http://www.uniprot.org/uniprot/GNAQ_HUMAN GNAQ_HUMAN]] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity. Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro) (By similarity).

== 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.

~~Authors~~:

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>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

== 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]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6vu5 is ON HOLD  until Feb 14 2022
+==Structure of G-alpha-q bound to its chaperone Ric-8A==
+<StructureSection load='6vu5' size='340' side='right'caption='[[6vu5]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6vu5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VU5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6VU5 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>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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=6vu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vu5 OCA], [http://pdbe.org/6vu5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vu5 RCSB], [http://www.ebi.ac.uk/pdbsum/6vu5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vu5 ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[[http://www.uniprot.org/uniprot/GNAQ_HUMAN GNAQ_HUMAN]] Sturge-Weber syndrome;Phakomatosis cesioflammea;Uveal melanoma;Familial multiple nevi flammei. The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.
+== Function ==
+[[http://www.uniprot.org/uniprot/GNAQ_HUMAN GNAQ_HUMAN]] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity. Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro) (By similarity).
+<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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6vu5" 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]]