Fig. 1 | Nature Communications

Fig. 1

From: A homologue of the Parkinson’s disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover

Fig. 1

The Chlorobium tepidum Roc-COR domain monomerizes upon binding of a non-hydrolysable GTP analogue (GppNHp). a Pairwise-comparison using CRYSOL of the theoretical scattering curve derived from the crystallographic dimer model of CtRoc-COR (PDB 3DPU, grey line) with the experimental scattering curves of CtRoc-COR in the absence of nucleotides (black dots) or in the presence of GDP (green dots) or GppNHp (red dots). b Superposition of the crystallographic CtRoc-COR dimer model (Roc in red and COR in blue) on the ab initio SAXS envelope, constructed starting from the scattering curve of CtRoc-COR in the absence of nucleotides. c Overview of the molecular masses obtained via SAXS (based on Porod volume/1.7), SEC-MALS and SV-AUC for CtRoc-COR in different nucleotide-bound states. The theoretical molecular mass of the monomer is given in between brackets. (NF = nucleotide-free) d SEC-MALS data for CtRoc-COR in the absence (black) or presence of nucleotides GDP (green) or GppNHp (red). e Native mass spectra of CtRoc-COR for the three different nucleotide states: nucleotide-free (NF), GDP-bound and GppNHp-bound. Peaks corresponding to dimeric and monomeric species are labeled with two circles and one circle, respectively

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