Structural principles for the propeller assembly of β‐sheets: The preference for seven‐fold symmetry

Publisher Website
Google Scholar
Abstract
Twisted β‐sheets, packed face to face, may be arranged in circular formation like blades of a propeller or turbine. This β‐pro‐peller fold has been found in three proteins: that in neuraminidase consists of six β‐sheets while those in methylamine dehydrogenase and galactose oxidase are composed of seven β‐sheets. A model for multisheet packing in the β‐propeller fold is proposed. This model gives both geometrical parameters of the β‐propellers composed of different numbers of sheets and patterns of residue packing at their sheet‐to‐sheet interfaces. All the known β‐propeller structures have been analyzed, and the observed geometries and residue packing are found to be in good agreement with those predicted by models. It is shown that unusual seven‐fold symmetry is preferable to six‐ or eight‐fold symmetry for propeller‐like multisheet assembly. According to the model, a six β‐sheet propeller has to have predominantly small residues in the β‐strands closed to its sixfold axis, but no strong sequence constraints are necessary for a seven‐fold β‐propeller.

This publication has 12 references indexed in Scilit: