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by Eric Martz
Coronavirus SARS-CoV-2 (responsible for COVID-19) has a spike protein on its surface, which enables it to infect host cells. Initially, proteases in the lungs clip the homo-trimeric spike protein at a unique sequence. This primes it, causing it to extend its receptor binding surface (shown in the above animation), optimizing binding to the host cell's ACE2 receptor (not shown). Next, spike protein initiates fusion of the virus and host cell membranes (not shown), enabling the virus RNA to enter the cell and initiate production of new virions. Knowledge of spike protein's molecular structure and function is crucial to developing effective therapies and vaccines.
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Y Gu, V Srikanth, AI Salazar-Morales, R Jain, JP O'Brien, SM Yi, RK Soni, FA Samatey, SE Yalcin, NS Malvankar. Nature 2021 doi: 10.1038/s41586-021-03857-w
Geobacter pili were long thought to be electrically conductive protein nanowires composed of PilA-N. Nanowires are crucial to the energy metabolism of bacteria flourishing in oxygen-deprived environments. To everyone's surprise, in 2019, the long-studied nanowires were found to be linear polymers of multi-heme cytochromes, not pili. The first cryo-EM structure of pili (2021) reveals a filament made of dimers of PilA-N and PilA-C, shown. Electrical conductivity of pili is much lower than that of cytochrome nanowires. Evidence suggests that PilA-NC filaments are periplasmic pseudopili crucial for exporting cytochrome nanowires onto the cell surface, rather than the pili serving as nanowires themselves.

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Above is a transmembrane protein that takes up, into your intestinal cells, orally consumed peptide nutrients and drugs. Its lumen-face (shown above) opens and binds peptide or drug, then closes, while its cytoplasmic face (opposite end from the above) opens to release its cargo into the intestinal cell, which passes it on into the blood circulation.

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