Mechanism of resilin elasticity.
Resilin is critical in the flight and jumping systems of insects as a polymeric rubber-like protein with outstanding elasticity. However, insight into the underlying molecular mechanisms responsible for resilin elasticity remains undefined. Here we report the structure and function of resilin from Drosophila CG15920. A reversible beta-turn transition was identified in the peptide encoded by exon III and for full-length resilin during energy input and release, features that correlate to the rapid deformation of resilin during functions in vivo. Micellar structures and nanoporous patterns formed after beta-turn structures were present via changes in either the thermal or the mechanical inputs. A model is proposed to explain the super elasticity and energy conversion mechanisms of resilin, providing important insight into structure-function relationships for this protein. Furthermore, this model offers a view of elastomeric proteins in general where beta-turn-related structures serve as fundamental units of the structure and elasticity.
Department of Biomedical Engineering, Tufts University, Medford, MA 02155, USA.
Guokui
G
Qin
Xiao
X
Hu
Peggy
P
Cebe
David L
DL
Kaplan
D000818:Animals; D029721:Drosophila Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004331:Drosophila melanogaster / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004548:Elasticity; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D013816:Thermodynamics
D029721:Drosophila Proteins; C577896:resilin protein, Drosophila