Structure and stability of designed TPR protein superhelices: unusual crystal packing and implications for natural TPR proteins.
作者： Tommi Kajander , Aitziber L. Cortajarena , Simon Mochrie , Lynne Regan
DOI: 10.1107/S0907444907024353
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摘要: The structure and stability of repeat proteins has been little studied in comparison to the properties more familiar globular proteins. Here, designed tetratricopeptide-repeat (TPR) is described. TPR a 34-amino-acid motif which adopts helix–turn–helix occurs as tandem repeats. design consensus (CTPR) previously crystal structures stabilities that contain eight or 20 identical repeats CTPR (CTPR8 CTPR20) are presented. Both CTPR8 CTPR20 adopt superhelical overall structure. different-length compared with each other natural domains. Also, unusual perhaps unique crystal-packing interactions resulting pseudo-infinite crystalline superhelices observed different forms discussed. Finally, it shown thermodynamic behavior can be predicted from TPRs this series using an Ising model-based analysis. protein CTPR2–CTPR20 covers size repertoire domains such excellent model system for
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