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| | <StructureSection load='5tdq' size='340' side='right'caption='[[5tdq]], [[Resolution|resolution]] 2.49Å' scene=''> | | <StructureSection load='5tdq' size='340' side='right'caption='[[5tdq]], [[Resolution|resolution]] 2.49Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5tdq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TDQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TDQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5tdq]] is a 1 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=5TDQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TDQ FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACBD3, GCP60, GOCAP1, GOLPH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 2.493Å</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=5tdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tdq OCA], [http://pdbe.org/5tdq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tdq RCSB], [http://www.ebi.ac.uk/pdbsum/5tdq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tdq ProSAT]</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=5tdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tdq OCA], [https://pdbe.org/5tdq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tdq RCSB], [https://www.ebi.ac.uk/pdbsum/5tdq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tdq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GCP60_HUMAN GCP60_HUMAN]] Involved in the maintenance of Golgi structure by interacting with giantin, affecting protein transport between the endoplasmic reticulum and Golgi. Involved in hormone-induced steroid biosynthesis in testicular Leydig cells (By similarity).<ref>PMID:11590181</ref> | + | [https://www.uniprot.org/uniprot/GCP60_HUMAN GCP60_HUMAN] Involved in the maintenance of Golgi structure by interacting with giantin, affecting protein transport between the endoplasmic reticulum and Golgi. Involved in hormone-induced steroid biosynthesis in testicular Leydig cells (By similarity).<ref>PMID:11590181</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Burke, J E]] | + | [[Category: Burke JE]] |
| - | [[Category: McPhail, J A]] | + | [[Category: McPhail JA]] |
| - | [[Category: Beta barrel]]
| + | |
| - | [[Category: Gold domain]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
GCP60_HUMAN Involved in the maintenance of Golgi structure by interacting with giantin, affecting protein transport between the endoplasmic reticulum and Golgi. Involved in hormone-induced steroid biosynthesis in testicular Leydig cells (By similarity).[1]
Publication Abstract from PubMed
Phosphatidylinositol 4-kinase III beta (PI4KIIIbeta) is an essential enzyme in mediating membrane transport, and plays key roles in facilitating viral infection. Many pathogenic positive-sense single-stranded RNA viruses activate PI4KIIIbeta to generate phosphatidylinositol 4-phosphate (PI4P)-enriched organelles for viral replication. The molecular basis for PI4KIIIbeta activation during viral infection has remained largely unclear. We describe the biochemical reconstitution and characterization of the complex of PI4KIIIbeta with the Golgi protein Acyl-coenzyme A binding domain containing protein 3 (ACBD3) and Aichi virus 3A protein on membranes. We find that 3A directly activates PI4KIIIbeta, and this activation is sensitized by ACBD3. The interfaces between PI4KIIIbeta-ACBD3 and ACBD3-3A were mapped with hydrogen-deuterium exchange mass spectrometry (HDX-MS). Determination of the crystal structure of the ACBD3 GOLD domain revealed a unique N terminus that mediates the interaction with 3A. Rationally designed complex-disrupting mutations in both ACBD3 and PI4KIIIbeta completely abrogated the sensitization of 3A activation by ACBD3.
The Molecular Basis of Aichi Virus 3A Protein Activation of Phosphatidylinositol 4 Kinase IIIbeta, PI4KB, through ACBD3.,McPhail JA, Ottosen EH, Jenkins ML, Burke JE Structure. 2016 Dec 7. pii: S0969-2126(16)30358-6. doi:, 10.1016/j.str.2016.11.016. PMID:27989622[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sohda M, Misumi Y, Yamamoto A, Yano A, Nakamura N, Ikehara Y. Identification and characterization of a novel Golgi protein, GCP60, that interacts with the integral membrane protein giantin. J Biol Chem. 2001 Nov 30;276(48):45298-306. Epub 2001 Oct 5. PMID:11590181 doi:http://dx.doi.org/10.1074/jbc.M108961200
- ↑ McPhail JA, Ottosen EH, Jenkins ML, Burke JE. The Molecular Basis of Aichi Virus 3A Protein Activation of Phosphatidylinositol 4 Kinase IIIbeta, PI4KB, through ACBD3. Structure. 2016 Dec 7. pii: S0969-2126(16)30358-6. doi:, 10.1016/j.str.2016.11.016. PMID:27989622 doi:http://dx.doi.org/10.1016/j.str.2016.11.016
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