8hf3

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(New page: '''Unreleased structure''' The entry 8hf3 is ON HOLD Authors: Description: Category: Unreleased Structures)
Current revision (05:56, 5 June 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 8hf3 is ON HOLD
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==Cryo-EM structure of human ZDHHC9/GCP16 complex==
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<StructureSection load='8hf3' size='340' side='right'caption='[[8hf3]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8hf3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HF3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HF3 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=PX2:1,2-DILAUROYL-SN-GLYCERO-3-PHOSPHATE'>PX2</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8hf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hf3 OCA], [https://pdbe.org/8hf3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hf3 RCSB], [https://www.ebi.ac.uk/pdbsum/8hf3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hf3 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/ZDHC9_HUMAN ZDHC9_HUMAN] Lujan-Fryns syndrome. The disease is caused by variants affecting the gene represented in this entry.
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== Function ==
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[https://www.uniprot.org/uniprot/ZDHC9_HUMAN ZDHC9_HUMAN] Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates, such as ADRB2, HRAS, NRAS and CGAS (PubMed:16000296, PubMed:27481942, PubMed:37802025). The ZDHHC9-GOLGA7 complex is a palmitoyltransferase specific for HRAS and NRAS (PubMed:16000296). May have a palmitoyltransferase activity toward the beta-2 adrenergic receptor/ADRB2 and therefore regulate G protein-coupled receptor signaling (PubMed:27481942). Acts as a regulator of innate immunity by catalyzing palmitoylation of CGAS, thereby promoting CGAS homodimerization and cyclic GMP-AMP synthase activity (PubMed:37802025).<ref>PMID:16000296</ref> <ref>PMID:27481942</ref> <ref>PMID:37802025</ref> (Microbial infection) Through a sequential action with ZDHHC20, rapidly and efficiently palmitoylates SARS coronavirus-2/SARS-CoV-2 spike protein following its synthesis in the endoplasmic reticulum (ER). In the infected cell, promotes spike biogenesis by protecting it from premature ER degradation, increases half-life and controls the lipid organization of its immediate membrane environment. Once the virus has formed, spike palmitoylation controls fusion with the target cell.<ref>PMID:34599882</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Palmitoylation of cysteine residues at the C-terminal hypervariable regions in human HRAS and NRAS, which is necessary for RAS signaling, is catalyzed by the acyltransferase DHHC9 in complex with its accessory protein GCP16. The molecular basis for the acyltransferase activity and the regulation of DHHC9 by GCP16 is not clear. Here we report the cryo-electron microscopy structures of the human DHHC9-GCP16 complex and its yeast counterpart-the Erf2-Erf4 complex, demonstrating that GCP16 and Erf4 are not directly involved in the catalytic process but stabilize the architecture of DHHC9 and Erf2, respectively. We found that a phospholipid binding to an arginine-rich region of DHHC9 and palmitoylation on three residues (C24, C25 and C288) were essential for the catalytic activity of the DHHC9-GCP16 complex. Moreover, we showed that GCP16 also formed complexes with DHHC14 and DHHC18 to catalyze RAS palmitoylation. These findings provide insights into the regulatory mechanism of RAS palmitoyltransferases.
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Authors:
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Regulation of RAS palmitoyltransferases by accessory proteins and palmitoylation.,Yang A, Liu S, Zhang Y, Chen J, Fan Y, Wang F, Zou Y, Feng S, Wu J, Hu Q Nat Struct Mol Biol. 2024 Mar;31(3):436-446. doi: 10.1038/s41594-023-01183-5. , Epub 2024 Jan 5. PMID:38182928<ref>PMID:38182928</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8hf3" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Hu Q]]
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[[Category: Liu S]]
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[[Category: Wu J]]
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[[Category: Yang A]]
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[[Category: Zhang Y]]

Current revision

Cryo-EM structure of human ZDHHC9/GCP16 complex

PDB ID 8hf3

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