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Aminoacyl-tRNA synthetases play a central role in assuring a high degree of accuracy in protein synthesis. New high resolution structures of threonyl-tRNA synthetase bound to threonine or a threonyl-adenylate analog reveal how an active site zinc atom contributes to translational fidelity.
A backbone model of ten subunits of yeast RNA polymerase II has been derived from the ongoing analysis of its crystal structure. Notable features include ‘jaws’ for holding DNA, a putatively RNA-regulated ‘sliding clamp’, two ‘pores’ located in the vicinity of the catalytic center, and a high degree of similarity with the structure of a bacterial RNA polymerase.
The complex between BMP-2, a TGF-β family member, and its high affinity receptor provides new insights into the assembly of receptor complexes for members of the cystine-knot growth factor family. A novel proposal for the interaction between Flt3L and its receptor suggests a general scheme for the interaction of closely related receptor tyrosine kinases with structurally diverse ligands, including certain members of the TGF-β family.
Formation of secondary structure during protein folding can now be probed on the submillisecond time scale. By monitoring the formation of α-helix formation during the initial collapse of cytochrome c, its folding mechanism is delineated.
The crystal structure of a lipid transfer START domain has been solved and shown to contain a hydrophobic tunnel that likely binds cholesterol. These results have implications for understanding the mechanism of action of the steroidogenic acute regulatory protein (StAR), which is indispensable in steroid biosynthesis.
