Anatomy and evolution of proteins displaying the viral capsid jellyroll topology.
In this paper the anatomy of 25 structures containing a jellyroll motif, consisting of eight antiparallel beta-strands forming a so-called beta-barrel, was investigated. This involved performing a careful structural alignment based on hydrogen bonds for the equivalent regions of the tertiary folds and a subsequent analysis of conserved amino acids, equivalenced residue-residue contacts, and various parameters describing the size, shape and other geometrical characteristics of these regions. It was found that the jellyroll motif is best viewed as a two-sheet wedge structure rather than a barrel. The more conserved parameters are discussed. A model of evolutionary development for the jellyroll fold in the various protein and viral structures is proposed.
Chelvanayagam
G
G
European Molecular Biology Laboratory, Heidelberg, Germany.
Heringa
J
J
Argos
P
P
D000595:Amino Acid Sequence; D005075:Biological Evolution; D002213:Capsid / Q000737:chemistry*; D006860:Hydrogen Bonding; D008969:Molecular Sequence Data; D017510:Protein Folding; D017433:Protein Structure, Secondary; D014961:X-Ray Diffraction