2mm4
From Proteopedia
Structure of a Conserved Golgi Complex-targeting Signal in Coronavirus Envelope Proteins
Structural highlights
FunctionVEMP_SARS Plays a central role in virus morphogenesis and assembly. Acts as a viroporin and self-assembles in host membranes forming pentameric protein-lipid pores that allow ion transport. Also plays a role in the induction of apoptosis (By similarity). Activates the host NLRP3 inflammasome, leading to IL-1beta overproduction.[HAMAP-Rule:MF_04204][1] [2] Publication Abstract from PubMedCoronavirus envelope (CoV E) proteins are approximately 100-residue polypeptides with at least one channel-forming alpha-helical transmembrane (TM) domain. The extramembrane C-terminal tail contains a completely conserved proline, at the center of a predicted beta-coil-beta motif. This hydrophobic motif has been reported to constitute a Golgi-targeting signal or a second TM domain. However, no structural data for this or other extramembrane domains in CoV E proteins is available. Herein, we show that the E protein in the severe acute respiratory syndrome virus has only one TM domain in micelles, whereas the predicted beta-coil-beta motif forms a short membrane-bound alpha-helix connected by a disordered loop to the TM domain. However, complementary results suggest that this motif is potentially poised for conformational change or in dynamic exchange with other conformations. Structure of a conserved Golgi complex-targeting signal in coronavirus envelope proteins.,Li Y, Surya W, Claudine S, Torres J J Biol Chem. 2014 May 2;289(18):12535-49. doi: 10.1074/jbc.M114.560094. Epub 2014, Mar 25. PMID:24668816[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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