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Revision as of 11:41, 18 October 2018

Welcome to Proteopedia
ISSN 2310-6301 The free, collaborative 3D-encyclopedia of proteins & other molecules

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Coronavirus COVID-19

A novel coronavirus was found to be the cause of a respiratory illness first detected in Wuhan, China in 2019. 3D structural studies are aiding scientists to understand how the coronavirus infects humans and helping to find new ways to treat the viral spread (video by Fusion Animation).

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Opening a Gate to Human Health

by Alice Clark (PDBe)
In the 1970s, an exciting discovery of a family of medicines was made by the Japanese scientist Satoshi Ōmura. One of these molecules, ivermectin, is shown in this artwork bound in the ligand binding pocket of the Farnesoid X receptor, a protein which helps regulate cholesterol in humans. This structure showed that ivermectin induced transcriptional activity of FXR and could be used to regulate metabolism.

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Geobacter nanowire structure surprise.

F Wang, Y Gu, JP O'Brien, SM Yi, SE Yalcin, V Srikanth, C Shen, D Vu, NL Ing, AI Hochbaum, EH Egelman, NS Malvankar. Cell 2019 doi: 10.1016/j.cell.2019.03.029
Bacteria living in anaerobic environments (no oxygen) need alternative electron acceptors in order to get energy from their food. An acceptor abundant in the earth's crust is red iron oxide ("rust"), which gets reduced to black iron oxide (magnetite). Many bacteria, such as Geobacter, get their metabolic energy by transferring electrons to acceptors that are multiple cell diameters distant, using protein nanowires. These were long thought to be pili. But when the structure of the nanowires was solved in 2019, to everyone's surprise, they turned out to be unprecedented linear polymers of multi-heme cytochromes. The hemes form an electrically conductive chain in the cores of these nanowires.

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Touch-Sensitive Channel

Touching stretches cell membranes, opening mechanosensitive ion channels, leading to sensation by the nervous system. Pictured is the transmembrane region of a similar channel in bacteria. When closed, the narrow opening is lined by hydrophobic amino acid sidechains, making it non-conductive to ions.

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Proteopedia Page Contributors and Editors (what is this?)

Joel L. Sussman, Jaime Prilusky

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