Solution structure of the ESCRT-I complex by small-angle X-ray scattering, EPR, and FRET spectroscopy
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11320%2F11%3A10105632" target="_blank" >RIV/00216208:11320/11:10105632 - isvavai.cz</a>
Result on the web
<a href="http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3111319/pdf/pnas.1101763108.pdf" target="_blank" >http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3111319/pdf/pnas.1101763108.pdf</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1073/pnas.1101763108" target="_blank" >10.1073/pnas.1101763108</a>
Alternative languages
Result language
angličtina
Original language name
Solution structure of the ESCRT-I complex by small-angle X-ray scattering, EPR, and FRET spectroscopy
Original language description
ESCRT-I is required for the sorting of integral membrane proteins to the lysosome, or vacuole in yeast, for cytokinesis in animal cells, and for the budding of HIV-1 from human macrophages and T lymphocytes. ESCRT-I is a heterotetramer of Vps23, Vps28, Vps37, and Mvb12. The crystal structures of the core complex and the ubiquitin E2 variant and Vps28 C-terminal domains have been determined, but internal flexibility has prevented crystallization of intact ESCRT-I. Here we have characterized the structureof ESCRT-I in solution by simultaneous structural refinement against small-angle X-ray scattering and double electron-electron resonance spectroscopy of spin-labeled complexes. An ensemble of at least six structures, comprising an equally populated mixture of closed and open conformations, was necessary to fit all of the data. This structural ensemble was cross-validated against single-molecule FRET spectroscopy, which suggested the presence of a continuum of open states. ESCRT-I in sol
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
BO - Biophysics
OECD FORD branch
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Result continuities
Project
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Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2011
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Proceedings of the National Academy of Sciences of the United States of America
ISSN
0027-8424
e-ISSN
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Volume of the periodical
108
Issue of the periodical within the volume
23
Country of publishing house
US - UNITED STATES
Number of pages
6
Pages from-to
9437-9442
UT code for WoS article
000291341400029
EID of the result in the Scopus database
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