Astrometric Very Long Baseline Interferometry (VLBI) observations of maser sources in the Milky Way are used to map the spiral structure of our Galaxy and to determine fundamental parameters such as the rotation velocity (Θ0) and curve and the distance to the Galactic center (R0). Here, we present an update on our first results, implementing a recent change in the knowledge about the Solar motion. It seems unavoidable that the IAU recommended values for R0 and Θ0 need a substantial revision. In particular the combination of 8.5 kpc and 220 km s −1 can be ruled out with high confidence. Combining the maser data with the distance to the Galactic center from stellar orbits and the proper motion of Sgr A* gives best values of R0 = 8.3 ± 0.23 kpc and Θ0 = 239 or 246 ± 7 km s −1 , for Solar motions of V = 12.23 and 5.25 km s −1 , respectively. Finally, we give an outlook to future observations in the Bar and Spiral Structure Legacy (BeSSeL) Survey.
A majority of the proteins targeted to the mitochondria are transported through the translocase of the outer membrane (TOM) complex. Tom70 is a major surface receptor for mitochondrial protein precursors in the TOM complex. To investigate how Tom70 receives the mitochondrial protein precursors, we have determined the crystal structure of yeast Tom70p to 3.0 A. Tom70p forms a homodimer in the crystal. Each subunit consists primarily of tetratricopeptide repeat (TPR) motifs, which are organized into a right-handed superhelix. The TPR motifs in the N-terminal domain of Tom70p form a peptide-binding groove for the C-terminal EEVD motif of Hsp70, whereas the C-terminal domain of Tom70p contains a large pocket that may be the binding site for mitochondrial precursors. The crystal structure of Tom70p provides insights into the mechanisms of precursor transport across the mitochondrion's outer membrane.
The flexibility and stability of organic solar cells (OSCs) have becoming a hotspot research for their practical applicaitons. Molecular arrangement and network morphology of active layer are important factors affecting...
Heat shock protein (Hsp) 40 facilitates the critical role of Hsp70 in a number of cellular processes such as protein folding, assembly, degradation and translocation in vivo. Hsp40 and Hsp70 stay in close contact to achieve these diverse functions. The conserved C-terminal EEVD motif in Hsp70 has been shown to regulate Hsp40-Hsp70 interaction by an unknown mechanism. Here, we provide a structural basis for this regulation by determining the crystal structure of yeast Hsp40 Sis1 peptide-binding fragment complexed with the Hsp70 Ssa1 C-terminal. The Ssa1 extreme C-terminal eight residues, G634PTVEEVD641, form a beta-strand with the domain I of Sis1 peptide-binding fragment. Surprisingly, the Ssa1 C-terminal binds Sis1 at the site where Sis1 interacts with the non-native polypeptides. The negatively charged residues within the EEVD motif in Ssa1 C-terminal form extensive charge-charge interactions with the positively charged residues in Sis1. The structure-based mutagenesis data support the structural observations.
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