7y96
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7y96]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria] and [https://en.wikipedia.org/wiki/Pipistrellus_bat_coronavirus_HKU5 Pipistrellus bat coronavirus HKU5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Y96 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Y96 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7y96]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria] and [https://en.wikipedia.org/wiki/Pipistrellus_bat_coronavirus_HKU5 Pipistrellus bat coronavirus HKU5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Y96 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Y96 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene></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]] 3.415Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene></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=7y96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7y96 OCA], [https://pdbe.org/7y96 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7y96 RCSB], [https://www.ebi.ac.uk/pdbsum/7y96 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7y96 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=7y96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7y96 OCA], [https://pdbe.org/7y96 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7y96 RCSB], [https://www.ebi.ac.uk/pdbsum/7y96 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7y96 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/VME1_BCHK5 VME1_BCHK5] Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins.[HAMAP-Rule:MF_04202][PROSITE-ProRule:PRU01275][https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. | [https://www.uniprot.org/uniprot/VME1_BCHK5 VME1_BCHK5] Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins.[HAMAP-Rule:MF_04202][PROSITE-ProRule:PRU01275][https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The membrane (M) protein is the most abundant structural protein of coronaviruses including MERS-CoV, SARS-CoV, and SARS-CoV-2, and plays a central role in virus assembly through its interaction with various partner proteins. However, mechanistic details about how M protein interacts with others remain elusive due to lack of high-resolution structures. Here, we present the first crystal structure of a betacoronavirus M protein from Pipistrellus bat coronavirus HKU5 (batCOV5-M), which is closely related to MERS-CoV, SARS-CoV, and SARS-CoV-2 M proteins. Furthermore, an interaction analysis indicates that the carboxy-terminus of the batCOV5 nucleocapsid (N) protein mediates its interaction with batCOV5-M. Combined with a computational docking analysis an M-N interaction model is proposed, providing insight into the mechanism of M protein-mediated protein interactions. | ||
| + | |||
| + | Crystal structure of the membrane (M) protein from a bat betacoronavirus.,Wang X, Yang Y, Sun Z, Zhou X PNAS Nexus. 2023 Jan 30;2(2):pgad021. doi: 10.1093/pnasnexus/pgad021. eCollection , 2023 Feb. PMID:36874273<ref>PMID:36874273</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7y96" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of the carboxy-terminal domain of a coronavirus M protein fused with a split GFP
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