Department of Biomedical Engineering, Tufts University, Medford, MA 02155, USA.
Nat Commun. 2012;3:1003. doi: 10.1038/ncomms2004.
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.
减震蛋白是昆虫飞行和跳跃系统的关键组成部分，它是一种具有杰出弹性的聚合橡胶状蛋白质。然而，减震蛋白弹性的潜在分子机制仍未得到明确的解释。在这里，我们报告了来自果蝇 CG15920 的减震蛋白的结构和功能。在能量输入和释放过程中，我们在编码外显子 III 的肽中鉴定出了一个可逆的β-转角转变，以及全长减震蛋白中的一个β-转角转变，这些特征与减震蛋白在体内功能过程中的快速变形相关。通过热或机械输入的变化，形成了β-转角结构后的胶束结构和纳米多孔模式。提出了一个模型来解释减震蛋白的超弹性和能量转换机制，为该蛋白的结构-功能关系提供了重要的见解。此外，该模型提供了一个关于弹性蛋白的一般观点，其中β-转角相关结构作为结构和弹性的基本单元。
