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| | <StructureSection load='6hlt' size='340' side='right'caption='[[6hlt]], [[Resolution|resolution]] 2.81Å' scene=''> | | <StructureSection load='6hlt' size='340' side='right'caption='[[6hlt]], [[Resolution|resolution]] 2.81Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6hlt]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Hrv-14 Hrv-14] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HLT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HLT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6hlt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rhinovirus_B14 Rhinovirus B14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HLT 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]] 2.815Å</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=6hlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hlt OCA], [http://pdbe.org/6hlt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hlt RCSB], [http://www.ebi.ac.uk/pdbsum/6hlt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hlt 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=6hlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hlt OCA], [https://pdbe.org/6hlt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hlt RCSB], [https://www.ebi.ac.uk/pdbsum/6hlt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hlt 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> [[http://www.uniprot.org/uniprot/POLG_HRV14 POLG_HRV14]] Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (By similarity). The capsid interacts with human ICAM1 to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis. VP0 precursor is a component of immature procapsids (By similarity). Protein 2A is a cysteine protease that is responsible for the cleavage between the P1 and P2 regions. It cleaves the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA transcription (By similarity). Protein 2B affects membrane integrity and cause an increase in membrane permeability (By similarity). Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity). Protein 3A, via its hydrophobic domain, serves as membrane anchor (By similarity). Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity). RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity). | + | [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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| | </div> | | </div> |
| | <div class="pdbe-citations 6hlt" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6hlt" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Human rhinovirus|Human rhinovirus]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Hrv-14]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Boura, E]] | + | [[Category: Rhinovirus B14]] |
| - | [[Category: Klima, M]] | + | [[Category: Boura E]] |
| - | [[Category: Complex]] | + | [[Category: Klima M]] |
| - | [[Category: Enterovirus]]
| + | |
| - | [[Category: Golgi]]
| + | |
| - | [[Category: Picornavirus]]
| + | |
| - | [[Category: Viral 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
Enteroviruses, members of the family of picornaviruses, are the most common viral infectious agents in humans causing a broad spectrum of diseases ranging from mild respiratory illnesses to life-threatening infections. To efficiently replicate within the host cell, enteroviruses hijack several host factors, such as ACBD3. ACBD3 facilitates replication of various enterovirus species, however, structural determinants of ACBD3 recruitment to the viral replication sites are poorly understood. Here, we present a structural characterization of the interaction between ACBD3 and the non-structural 3A proteins of four representative enteroviruses (poliovirus, enterovirus A71, enterovirus D68, and rhinovirus B14). In addition, we describe the details of the 3A-3A interaction causing the assembly of the ACBD3-3A heterotetramers and the interaction between the ACBD3-3A complex and the lipid bilayer. Using structure-guided identification of the point mutations disrupting these interactions, we demonstrate their roles in the intracellular localization of these proteins, recruitment of downstream effectors of ACBD3, and facilitation of enterovirus replication. These structures uncovered a striking convergence in the mechanisms of how enteroviruses and kobuviruses, members of a distinct group of picornaviruses that also rely on ACBD3, recruit ACBD3 and its downstream effectors to the sites of viral replication.
Convergent evolution in the mechanisms of ACBD3 recruitment to picornavirus replication sites.,Horova V, Lyoo H, Rozycki B, Chalupska D, Smola M, Humpolickova J, Strating JRPM, van Kuppeveld FJM, Boura E, Klima M PLoS Pathog. 2019 Aug 5;15(8):e1007962. doi: 10.1371/journal.ppat.1007962. PMID:31381608[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
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
- ↑ Horova V, Lyoo H, Rozycki B, Chalupska D, Smola M, Humpolickova J, Strating JRPM, van Kuppeveld FJM, Boura E, Klima M. Convergent evolution in the mechanisms of ACBD3 recruitment to picornavirus replication sites. PLoS Pathog. 2019 Aug 5;15(8):e1007962. doi: 10.1371/journal.ppat.1007962. PMID:31381608 doi:http://dx.doi.org/10.1371/journal.ppat.1007962
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