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@article{2384837,
author = {Farci, Domenica and Haniewicz, Patrycja and Daniele, de Sanctis and Iesu, Luca and Kereiche, Sami and Winterhalter, Mathias and Piano, Dario},
article_location = {AMSTERDAM},
article_number = {6},
doi = {http://dx.doi.org/10.1016/j.jbc.2022.102031},
keywords = {PROTEINS; MICROSCOPE; RESOLUTION; Deinococcus radiodurans; S-layer; deinoxanthin-binding complex;},
language = {eng},
issn = {1083-351X},
journal = {International Journal of Biological Chemistry},
title = {The cryo-EM structure of the S-layer deinoxanthin-binding complex of<i> Deinococcus</i><i> radiodurans</i> informs properties of its environmental interactions},
url = {https://www.sciencedirect.com/science/article/pii/S0021925822004719?via%3Dihub},
volume = {298},
year = {2022}
}
TY - JOUR
ID - 2384837
AU - Farci, Domenica - Haniewicz, Patrycja - Daniele, de Sanctis - Iesu, Luca - Kereiche, Sami - Winterhalter, Mathias - Piano, Dario
PY - 2022
TI - The cryo-EM structure of the S-layer deinoxanthin-binding complex of<i> Deinococcus</i><i> radiodurans</i> informs properties of its environmental interactions
JF - International Journal of Biological Chemistry
VL - 298
IS - 6
SP - 1-8
EP - 1-8
PB - ANSInet
SN - 1083351X
KW - PROTEINS
KW - MICROSCOPE
KW - RESOLUTION
KW - Deinococcus radiodurans
KW - S-layer
KW - deinoxanthin-binding complex;
UR - https://www.sciencedirect.com/science/article/pii/S0021925822004719?via%3Dihub
N2 - The radiation-resistant bacterium Deinococcus radiodurans is known as the world's toughest bacterium. The S-layer of D. radiodurans, consisting of several proteins on the surface of the cellular envelope and intimately associated with the outer membrane, has therefore been useful as a model for structural and functional studies. Its main proteinaceous unit, the S-layer deinoxanthin-binding complex (SDBC), is a hetero-oligomeric assembly known to contribute to the resistance against environmental stress and have porin functional features; however, its precise structure is unknown. Here, we resolved the structure of the SDBC at -2.5 angstrom resolution by cryo-EM and assigned the sequence of its main subunit, the protein DR_2577. This structure is characterized by a pore region, a massive beta-barrel organization, a stalk region consisting of a trimeric coiled coil, and a collar region at the base of the stalk. We show that each monomer binds three Cu ions and one Fe ion and retains one deinoxanthin molecule and two phosphoglycolipids, all exclusive to D. radiodurans. Finally, electrophysiological characterization of the SDBC shows that it exhibits transport properties with several amino acids. Taken together, these results highlight the SDBC as a robust structure displaying both protection and sieving functions that facilitates exchanges with the environment.
ER -
FARCI, Domenica, Patrycja HANIEWICZ, de Sanctis DANIELE, Luca IESU, Sami KEREICHE, Mathias WINTERHALTER and Dario PIANO. The cryo-EM structure of the S-layer deinoxanthin-binding complex of\&{}lt;i\&{}gt; Deinococcus\&{}lt;/i\&{}gt;\&{}lt;i\&{}gt; radiodurans\&{}lt;/i\&{}gt; informs properties of its environmental interactions. \textit{International Journal of Biological Chemistry}. AMSTERDAM: ANSInet, 2022, vol.~298, No~6, p.~1-8. ISSN~1083-351X. Available from: https://dx.doi.org/10.1016/j.jbc.2022.102031.
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