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@ARTICLE{Schwarten:9748,
      author       = {Schwarten, M. and Stoldt, M. and Mohrlüder, J. and
                      Willbold, D.},
      title        = {{S}olution structure of {A}tg8 reveals conformational
                      polymorphism of the {N}-terminal domain},
      journal      = {Biochemical and biophysical research communications},
      volume       = {395},
      issn         = {0006-291X},
      address      = {Orlando, Fla.},
      publisher    = {Academic Press},
      reportid     = {PreJuSER-9748},
      pages        = {426 - 431},
      year         = {2010},
      note         = {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).},
      abstract     = {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.},
      keywords     = {Autophagy / Microtubule-Associated Proteins: chemistry /
                      Nuclear Magnetic Resonance, Biomolecular / Protein Folding /
                      Protein Structure, Tertiary / Saccharomyces cerevisiae:
                      chemistry / Saccharomyces cerevisiae: physiology /
                      Saccharomyces cerevisiae Proteins: chemistry / Ubiquitin:
                      chemistry / ATG8 protein, S cerevisiae (NLM Chemicals) /
                      Microtubule-Associated Proteins (NLM Chemicals) /
                      Saccharomyces cerevisiae Proteins (NLM Chemicals) /
                      Ubiquitin (NLM Chemicals) / J (WoSType)},
      cin          = {ISB-3 / JARA-HPC},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB942 / $I:(DE-82)080012_20140620$},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:20382112},
      UT           = {WOS:000277801200026},
      doi          = {10.1016/j.bbrc.2010.04.043},
      url          = {https://juser.fz-juelich.de/record/9748},
}