Structural analysis of the architecture and in situ localization of the main S-layer complex in Deinococcus radiodurans
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11110%2F21%3A10434580" target="_blank" >RIV/00216208:11110/21:10434580 - isvavai.cz</a>
Result on the web
<a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=MRk4RYipk-" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=MRk4RYipk-</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.str.2021.06.014" target="_blank" >10.1016/j.str.2021.06.014</a>
Alternative languages
Result language
angličtina
Original language name
Structural analysis of the architecture and in situ localization of the main S-layer complex in Deinococcus radiodurans
Original language description
Bacterial surface layers are paracrystalline assemblies of proteins that provide the first line of defense against environmental shocks. Here, we report the 3D structure, in situ localization, and orientation of the S-layer deinoxanthin-binding complex (SDBC), a hetero-oligomeric assembly of proteins that in Deinococcus radiodurans represents the main S-layer unit. The SDBC is resolved at 11-angstrom resolution by single-particle analysis, while its in situ localization is determined by cryo-electron crystallography on intact cell-wall fragments leading to a projection map at 4.5-angstrom resolution. The SDBC exhibits a triangular base with three comma-shaped pores, and a stalk departing orthogonally from the center of the base and oriented toward the intracellular space. Combining state-of-the-art techniques, results show the organization of this S-layer and its connection within the underlying membranes, demonstrating the potential for applications from nanotechnologies to medicine.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10600 - Biological sciences
Result continuities
Project
<a href="/en/project/GJ18-25144Y" target="_blank" >GJ18-25144Y: Structural exploration of the ATP-dependent human mitochondrial Lon protease for drug design and further understanding of its mechanism of action</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Structure
ISSN
0969-2126
e-ISSN
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Volume of the periodical
29
Issue of the periodical within the volume
11
Country of publishing house
GB - UNITED KINGDOM
Number of pages
11
Pages from-to
1279-"1285.e3"
UT code for WoS article
000718037100008
EID of the result in the Scopus database
2-s2.0-85115642386