Please use this identifier to cite or link to this item:
|Title:||Morphogenesis of the T4 tail and tail fibers||Authors:||Leiman, P.G.
Van Raaij, M.J.
|Issue Date:||2010||Citation:||Leiman, P.G., Arisaka, F., Van Raaij, M.J., Kostyuchenko, V.A., Aksyuk, A.A., Kanamaru, S., Rossmann, M.G. (2010). Morphogenesis of the T4 tail and tail fibers. Virology Journal 7 : -. ScholarBank@NUS Repository. https://doi.org/10.1186/1743-422X-7-355||Abstract:||Remarkable progress has been made during the past ten years in elucidating the structure of the bacteriophage T4 tail by a combination of three-dimensional image reconstruction from electron micrographs and X-ray crystallography of the components. Partial and complete structures of nine out of twenty tail structural proteins have been determined by X-ray crystallography and have been fitted into the 3D-reconstituted structure of the "extended" tail. The 3D structure of the "contracted" tail was also determined and interpreted in terms of component proteins. Given the pseudo-atomic tail structures both before and after contraction, it is now possible to understand the gross conformational change of the baseplate in terms of the change in the relative positions of the subunit proteins. These studies have explained how the conformational change of the baseplate and contraction of the tail are related to the tail's host cell recognition and membrane penetration function. On the other hand, the baseplate assembly process has been recently reexamined in detail in a precise system involving recombinant proteins (unlike the earlier studies with phage mutants). These experiments showed that the sequential association of the subunits of the baseplate wedge is based on the induced-fit upon association of each subunit. It was also found that, upon association of gp53 (gene product 53), the penultimate subunit of the wedge, six of the wedge intermediates spontaneously associate to form a baseplate-like structure in the absence of the central hub. Structure determination of the rest of the subunits and intermediate complexes and the assembly of the hub still require further study. © 2010 Leiman et al; licensee BioMed Central Ltd.||Source Title:||Virology Journal||URI:||http://scholarbank.nus.edu.sg/handle/10635/124868||ISSN:||1743422X||DOI:||10.1186/1743-422X-7-355|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Jan 21, 2022
WEB OF SCIENCETM
checked on Jan 21, 2022
checked on Jan 20, 2022
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.