The phage lambda major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system. Pell Lisa G,Kanelis Voula,Donaldson Logan W,Howell P Lynne,Davidson Alan R. Proceedings of the National Academy of Sciences of the United States of America...
R. The phage λ major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system. Proc. Natl Acad. Sci. USA 106, 4160–4165 (2009). Article CAS PubMed PubMed Central Google Scholar Wang, C., Tu, J., Liu, J. & Molineux, I...
摘要: The crystal structure of bacteriophage P22 tailspike protein reveals a striking fold with a distinctive, fish-like appearance, and helps explain many of the properties of this unusual molecule and its folding pathway.关键词: AMYLASE ACTIVITY CADMIUM CHLORIDE CARBOHYDRATE METABOLISM CRAYFISH ...
Among these are type VI secretion systems, insecticidal protein complexes, and bacteriocins. Phage tail-like bacteriocins (PTLBs) are widespread in bacteria, comprising different types that likely evolved independently. They can be divided into two major classes: the R-type PTLBs, which are related...
Phage-particle polypeptides P7 (molecular weight 33,000) and P11 (molecular weight 16,000) were identified as major head proteins and P10 (molecular weight 26,000) was shown to be the major tail protein. A DNA-free head-like structure containing P7 but not P11 was present in wild-type ...
(2009). The phage lambda major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system. Proc Natl Acad Sci USA 106: 4160–4165. Salmon KA, Freedman O, Ritchings BW, DuBow MS. (2000). Characterization of the lysogenic repressor (...
In case major coat protein pVIII is used for display, a polyvalent display takes place with the peptide displayed on each of the 2700 pVIII coat proteins. Because of the multiple copies of the displayed peptide, the avidity effect is probably more significant than the affinity effect during ...
(protein structure in blue) is conserved at the phage genus level whereas the structure of the C-terminal RBD (protein structure in red) clusters per O-antigen serogroup, illustrating a HGT across genera substrate binding site, as has been described for some tail ...
R. The phage lambda major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system. Proc Natl Acad Sci 106, 4160–4165, doi: 10.1073/pnas.0900044106 (2009). 51. Dieterle, M. E. et al. Exposing the secrets of two well-known ...
Type VI secretion systems and tailocins, two bacterial phage tail-like particles, have been reported to foster interbacterial competition. Both nanostructures enable their producer to kill other bacteria competing for the same ecological niche. Previously, type VI secretion systems and particularly R-...