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| Hauptseite > Publikationsdatenbank > Solution structure of Atg8 reveals conformational polymorphism of the N-terminal domain > print |
| Hauptseite > Publikationsdatenbank > Solution structure of Atg8 reveals conformational polymorphism of the N-terminal domain > print |
| 001 | 9748 | ||
| 005 | 20200402205832.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:20382112 |
| 024 | 7 | _ | |2 DOI |a 10.1016/j.bbrc.2010.04.043 |
| 024 | 7 | _ | |2 WOS |a WOS:000277801200026 |
| 037 | _ | _ | |a PreJuSER-9748 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 084 | _ | _ | |2 WoS |a Biochemistry & Molecular Biology |
| 084 | _ | _ | |2 WoS |a Biophysics |
| 100 | 1 | _ | |0 P:(DE-HGF)0 |a Schwarten, M. |b 0 |
| 245 | _ | _ | |a Solution structure of Atg8 reveals conformational polymorphism of the N-terminal domain |
| 260 | _ | _ | |a Orlando, Fla. |b Academic Press |c 2010 |
| 300 | _ | _ | |a 426 - 431 |
| 336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a article |2 DRIVER |
| 440 | _ | 0 | |0 787 |a Biochemical and Biophysical Research Communications |v 395 |x 0006-291X |y 7 |
| 500 | _ | _ | |a We thank Sameer Singh for carefully reading the manuscript as well as Clara Gruning, Justin Lecher and Sven Schunke for helpful discussions. This study was supported by a fellowship of the International Helmholtz Research School of Biophysics and Soft Matter (IHRS BioSoft) to M. Schwarten and a research Grant from the Deutsche Forschungsgemeinschaft (DFG) to D. Willbold (Wi1472/5). |
| 520 | _ | _ | |a During autophagy a crescent shaped like membrane is formed, which engulfs the material that is to be degraded. This membrane grows further until its edges fuse to form the double membrane covered autophagosome. Atg8 is a protein, which is required for this initial step of autophagy. Therefore, a multistage conjugation process of newly synthesized Atg8 to phosphatidylethanolamine is of critical importance. Here we present the high resolution structure of unprocessed Atg8 determined by nuclear magnetic resonance spectroscopy. Its C-terminal subdomain shows a well-defined ubiquitin-like fold with slightly elevated mobility in the pico- to nanosecond timescale as determined by heteronuclear NOE data. In comparison to unprocessed Atg8, cleaved Atg8(G116) shows a decreased mobility behaviour. The N-terminal domain adopts different conformations within the micro- to millisecond timescale. The possible biological relevance of the differences in dynamic behaviours between both subdomains as well as between the cleaved and uncleaved forms is discussed. |
| 536 | _ | _ | |0 G:(DE-Juel1)FUEK409 |2 G:(DE-HGF) |a Funktion und Dysfunktion des Nervensystems |c P33 |x 0 |
| 536 | _ | _ | |0 G:(DE-Juel1)FUEK505 |2 G:(DE-HGF) |a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung |c P45 |x 1 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Autophagy |
| 650 | _ | 2 | |2 MeSH |a Microtubule-Associated Proteins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Nuclear Magnetic Resonance, Biomolecular |
| 650 | _ | 2 | |2 MeSH |a Protein Folding |
| 650 | _ | 2 | |2 MeSH |a Protein Structure, Tertiary |
| 650 | _ | 2 | |2 MeSH |a Saccharomyces cerevisiae: chemistry |
| 650 | _ | 2 | |2 MeSH |a Saccharomyces cerevisiae: physiology |
| 650 | _ | 2 | |2 MeSH |a Saccharomyces cerevisiae Proteins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Ubiquitin: chemistry |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a ATG8 protein, S cerevisiae |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Microtubule-Associated Proteins |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Saccharomyces cerevisiae Proteins |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Ubiquitin |
| 650 | _ | 7 | |2 WoSType |a J |
| 653 | 2 | 0 | |2 Author |a Atg8 |
| 653 | 2 | 0 | |2 Author |a Autophagy |
| 653 | 2 | 0 | |2 Author |a NMR spectroscopy |
| 653 | 2 | 0 | |2 Author |a Dynamics |
| 653 | 2 | 0 | |2 Author |a GABARAP-like family |
| 653 | 2 | 0 | |2 Author |a Oligomerization |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Stoldt, M. |b 1 |
| 700 | 1 | _ | |0 P:(DE-Juel1)132012 |a Mohrlüder, J. |b 2 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-Juel1)132029 |a Willbold, D. |b 3 |u FZJ |
| 773 | _ | _ | |0 PERI:(DE-600)1461396-7 |a 10.1016/j.bbrc.2010.04.043 |g Vol. 395, p. 426 - 431 |p 426 - 431 |q 395<426 - 431 |t Biochemical and biophysical research communications |v 395 |x 0006-291X |y 2010 |
| 909 | C | O | |o oai:juser.fz-juelich.de:9748 |p VDB |
| 913 | 1 | _ | |0 G:(DE-Juel1)FUEK409 |a DE-HGF |b Gesundheit |k P33 |l Funktion und Dysfunktion des Nervensystems |v Funktion und Dysfunktion des Nervensystems |x 0 |
| 913 | 1 | _ | |0 G:(DE-Juel1)FUEK505 |a DE-HGF |b Schlüsseltechnologien |k P45 |l Biologische Informationsverarbeitung |v BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung |x 1 |
| 914 | 1 | _ | |y 2010 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
| 920 | 1 | _ | |d 31.12.2010 |g ISB |k ISB-3 |l Strukturbiochemie |0 I:(DE-Juel1)VDB942 |x 0 |
| 920 | 1 | _ | |0 I:(DE-82)080012_20140620 |k JARA-HPC |l Jülich Aachen Research Alliance - High-Performance Computing |g JARA |x 1 |
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| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
| 980 | _ | _ | |a I:(DE-82)080012_20140620 |
| 980 | _ | _ | |a UNRESTRICTED |
| 981 | _ | _ | |a I:(DE-Juel1)IBI-7-20200312 |
| 981 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
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