We report here the selection of DARPins directed against a macromolecular multiprotein complex, the baseplate BppUBppL complex of the lactococcal phage TP901-1. Using ribosome display, we selected several DARP1ns that bound specifically to the tip of the receptor-binding protein (RBP, the BppL...
(2012). Structure of the phage TP901-1 1.8 MDa baseplate suggests an alternative host adhesion mechanism. Proc. Natl. Acad. Sci. U.S.A. 109, 8954... Veesler,Spinelli,Mahony,... 被引量: 0发表: 0年 Type VI secretion system translocates a phage tail spike-like protein into target cells...
et al. Structure and molecular assignment of lactococcal phage TP901-1 baseplate. J Biol Chem 285, 39079–39086, doi: 10.1074/jbc.M110.175646 (2010). 35. Krogh, A., Larsson, B., von Heijne, G. & Sonnhammer, E. L. Predicting transmembrane protein topology with a hidden Markov model:...
2006. Identification of the lower baseplate protein as the antire- ceptor of the temperate lactococcal bacteriophages TP901-1 and Tuc2009. J. Bacteriol. 188:55- 63.Vegge CS, Vogensen FK, Mc Grath S, Neve H, van Sinderen D, Brondsted L: Identification of the lower baseplate protein as...
We report here the selection of DARPins directed against a macromolecular multiprotein complex, the baseplate BppUxBppL complex of the lactococcal phage TP901-1. Using ribosome display, we selected several DARPins that bound specifically to the tip of the receptor-binding protein (RBP, the BppL...
Here, we extend this approach and employ AlphaFold2 to determine the structure of a complete phage, the lactococcal P335 phage TP901-1. Herein we report the structures of its capsid and neck, its extended tail, and the complete adhesion device, the baseplate, which was previously partially ...