Protein Science, Vol 9, Issue 12 2338-2343, Copyright © 2000 by Cold Spring Harbor Laboratory Press

JOURNAL ARTICLE

Beta-helix core packing within the triple-stranded oligomerization domain of the P22 tailspike

JF Kreisberg, SD Betts and J King
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139, USA.

A right-handed parallel beta-helix of 400 residues in 13 tightly packed coils is a major motif of the chains forming the trimeric P22 tailspike adhesin. The beta-helix domains of three identical subunits are side-by-side in the trimer and make predominantly hydrophilic inter-subunit contacts (Steinbacher S et al., 1994, Science 265:383-386). After the 13th coil the three individual beta-helices terminate and the chains wrap around each other to form three interdigitated beta-sheets organized into the walls of a triangular prism. The beta-strands then separate and form antiparallel beta-sheets, but still defining a triangular prism in which each side is a beta-sheet from a different subunit (Seckler R, 1998, J Struct Biol 122:216-222). The subunit interfaces are buried in the triangular core of the prism, which is densely packed with hydrophobic side chains from the three beta-sheets. Examination of this structure reveals that its packed core maintains the same pattern of interior packing found in the left-handed beta-helix, a single-chain structure. This packing is maintained in both the interdigitated parallel region of the prism and the following antiparallel sheet section. This oligomerization motif for the tailspike beta-helices presumably contributes to the very high thermal and detergent stability that is a property of the native tailspike adhesin.
CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				M. Jain, M. S. Evans, J. King, and P. L. Clark Monoclonal Antibody Epitope Mapping Describes Tailspike {beta}-Helix Folding and Aggregation Intermediates J. Biol. Chem., June 17, 2005; 280(24): 23032 - 23040. [Abstract] [Full Text] [PDF]

				S. Betts, C. Haase-Pettingell, K. Cook, and J. King Buried hydrophobic side-chains essential for the folding of the parallel {beta}-helix domains of the P22 tailspike Protein Sci., September 1, 2004; 13(9): 2291 - 2303. [Abstract] [Full Text] [PDF]

				M. J. Gage and A. S. Robinson C-terminal hydrophobic interactions play a critical role in oligomeric assembly of the P22 tailspike trimer Protein Sci., December 1, 2003; 12(12): 2732 - 2747. [Abstract] [Full Text] [PDF]

				J. F. Kreisberg, S. D. Betts, C. Haase-Pettingell, and J. King The interdigitated {beta}-helix domain of the P22 tailspike protein acts as a molecular clamp in trimer stabilization Protein Sci., April 1, 2002; 11(4): 820 - 830. [Abstract] [Full Text] [PDF]

				P. Bradley, L. Cowen, M. Menke, J. King, and B. Berger BETAWRAP: Successful prediction of parallel beta -helices from primary sequence reveals an association with many microbial pathogens PNAS, December 18, 2001; 98(26): 14819 - 14824. [Abstract] [Full Text] [PDF]

				P. L. Clark and J. King A Newly Synthesized, Ribosome-bound Polypeptide Chain Adopts Conformations Dissimilar from Early in Vitro Refolding Intermediates J. Biol. Chem., June 29, 2001; 276(27): 25411 - 25420. [Abstract] [Full Text] [PDF]