Journal Article

PreJuSER-7510

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Comparative modeling of human NSF reveals a possible binding mode of GABARAP and GATE-16

Thielmann, Y.FZJ* ; Weiergräber, O. H.FZJ* ; Ma, P.FZJ* ; Schwarten, M.FZJ* ; Mohrlüder, J.FZJ* ; Willbold, D.FZJ*

2009
Wiley-Liss New York, NY

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Please use a persistent id in citations: doi:10.1002/prot.22477

Abstract: Vesicular trafficking is an important homeostatic process in eukaryotic cells which critically relies on membrane fusion. One of the essential components of the universal membrane fusion machinery is NSF (N-ethylmaleimide-sensitive factor), a large hexameric ATPase involved in disassembly of SNARE (soluble NSF attachment protein receptor) complexes. To improve our understanding of this sophisticated molecular machine, we have modeled the structure of the NSF hexamer in two alternative assemblies. Our data suggest a mechanistic concept of the operating mode of NSF which helps to explain the functional impact of post-translational modifications and mutations reported previously. Furthermore, we propose a binding site for the ubiquitin-like proteins GABARAP and GATE-16, which is supported by experimental evidence, yielding a complex with favorable surface complementarity.

Keyword(s): Adaptor Proteins, Signal Transducing: chemistry (MeSH) ; Adenosine Triphosphate: chemistry (MeSH) ; Binding Sites (MeSH) ; Humans (MeSH) ; Hydrolysis (MeSH) ; Microfilament Proteins: chemistry (MeSH) ; Microtubule-Associated Proteins: chemistry (MeSH) ; Models, Molecular (MeSH) ; N-Ethylmaleimide-Sensitive Proteins: chemistry (MeSH) ; Peptides: chemistry (MeSH) ; Phosphorylation (MeSH) ; Protein Binding (MeSH) ; Protein Conformation (MeSH) ; Protein Interaction Mapping (MeSH) ; Protein Structure, Tertiary (MeSH) ; Ubiquitin: chemistry (MeSH) ; Adaptor Proteins, Signal Transducing ; GABARAP protein, human ; GABARAPL2 protein, human ; Microfilament Proteins ; Microtubule-Associated Proteins ; Peptides ; Ubiquitin ; Adenosine Triphosphate ; N-Ethylmaleimide-Sensitive Proteins ; J ; N-ethylmaleimide-sensitive factor (auto) ; GABARAP (auto) ; comparative modeling (auto) ; structure model (auto) ; protein-protein interaction (auto)

Note: Grant sponsor: Deutsche Forschungsgememschaft (DFG); Grant number: Wil472/5.

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Contributing Institute(s):

1. Molekulare Biophysik (ISB-2)

Research Program(s):

1. Programm Biosoft (N03)

Appears in the scientific report 2009

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