j 2023

The SDBC is active in quenching oxidative conditions and the cell in <i>Deinococcus radiodurans</i>

FARCI, Domenica, Andre T GRACA, Luca IESU, de Sanctis DANIELE, Dario PIANO et. al.

Základní údaje

Originální název

The SDBC is active in quenching oxidative conditions and the cell in <i>Deinococcus radiodurans</i>

Autoři

FARCI, Domenica (garant), Andre T GRACA, Luca IESU, de Sanctis DANIELE a Dario PIANO

Vydání

International Journal of Biological Chemistry, AMSTERDAM, ANSInet, 2023, 1819-155X

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku (nerecenzovaný)

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Odkazy

Kód RIV

RIV/00216224:90242/23:00133745

Organizační jednotka

CIISB III

DOI

UT WoS

001016293500001

Klíčová slova anglicky

Deinococcus radiodurans; S-layer Deinoxanthin-binding complex; cryo-EM; superoxide dismutase (SOD);

Štítky

Příznaky

Mezinárodní význam
Změněno: 11. 4. 2024 23:24, Mgr. Michal Petr

Anotace

V originále

Deinococcus radiodurans is known for its remarkable ability to withstand harsh stressful conditions. The outermost layer of its cell envelope is a proteinaceous coat, the S-layer, essential for resistance to and interactions with the environment. The S-layer Deinoxanthin-binding complex (SDBC), one of the main units of the characteristic multilayered cell envelope of this bacterium, protects against environmental stressors and allows exchanges with the environment. So far, specific regions of this complex, the collar and the stalk, remained unassigned. Here, these regions are resolved by cryo-EM and locally refined. The resulting 3D map shows that the collar region of this multiprotein complex is a trimer of the protein DR_0644, a Cu only superoxide dismutase (SOD) identified here to be efficient in quenching reactive oxygen species. The same data also showed that the stalk region consists of a coiled coil that extends into the cell envelope for 280 Å, reaching the inner membrane. Finally, the orientation and localization of the complex are defined by in situ cryo-electron crystallography. The structural organization of the SDBC couples fundamental UV antenna properties with the presence of a Cu-only SOD, showing here coexisting photoprotective and chemoprotective functions. These features suggests how the SDBC and similar protein complexes, might have played a primary role as evol utive templates for the origin of photoautotrophic processes by combining primary protective needs with more independent energetic strategies.

Návaznosti

90242, velká výzkumná infrastruktura
Název: CIISB III