ORF8a of SARS-CoV forms an ion channel: experiments and molecular dynamics simulations.
ORF8a protein is 39 residues long and contains a single transmembrane domain. The protein is synthesized using solid phase peptide synthesis and reconstituted into artificial lipid bilayers that forms cation-selective ion channels with a main conductance level of 8.9±0.8pS at elevated temperature (38.5°C). Computational modeling studies including multi nanosecond molecular dynamics simulations in a hydrated POPC lipid bilayer are done with a 22 amino acid transmembrane helix to predict a putative homooligomeric helical bundle model. A structural model of a pentameric bundle is proposed with cysteines, serines and threonines facing the pore.
Chen
Cheng-Chang
CC
Institute of Biophotonics, School of Biomedical Science and Engineering, National Yang-Ming University, 155, Li-Nong St., Sec. 2, Taipei, 112, Taiwan.
Krüger
Jens
J
Sramala
Issara
I
Hsu
Hao-Jen
HJ
Henklein
Peter
P
Chen
Yi-Ming Arthur
YM
Fischer
Wolfgang B
WB
D000595:Amino Acid Sequence; D003198:Computer Simulation; D007473:Ion Channels / Q000737:chemistry* / Q000235:genetics; D008051:Lipid Bilayers; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D045473:Severe acute respiratory syndrome-related coronavirus / Q000737:chemistry* / Q000235:genetics; D014763:Viral Matrix Proteins / Q000737:chemistry* / Q000235:genetics
D007473:Ion Channels; D008051:Lipid Bilayers; D014763:Viral Matrix Proteins; C488151:sars7a protein, SARS virus