2FO7
Crystal structure of an 8 repeat consensus TPR superhelix (trigonal crystal form)
2FO7 の概要
エントリーDOI | 10.2210/pdb2fo7/pdb |
関連するPDBエントリー | 2AVP |
分子名称 | SYNTHETIC CONSENSUS TPR PROTEIN, CADMIUM ION (3 entities in total) |
機能のキーワード | tetratricopeptide repeat, tpr, consensus protein, superhelix, de novo protein |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 16376.06 |
構造登録者 | |
主引用文献 | Kajander, T.,Cortajarena, A.L.,Mochrie, S.,Regan, L. Structure and stability of designed TPR protein superhelices: unusual crystal packing and implications for natural TPR proteins. Acta Crystallogr.,Sect.D, 63:800-811, 2007 Cited by PubMed Abstract: The structure and stability of repeat proteins has been little studied in comparison to the properties of the more familiar globular proteins. Here, the structure and stability of designed tetratricopeptide-repeat (TPR) proteins is described. The TPR is a 34-amino-acid motif which adopts a helix-turn-helix structure and occurs as tandem repeats. The design of a consensus TPR motif (CTPR) has previously been described. Here, the crystal structures and stabilities of proteins that contain eight or 20 identical tandem repeats of the CTPR motif (CTPR8 and CTPR20) are presented. Both CTPR8 and CTPR20 adopt a superhelical overall structure. The structures of the different-length CTPR proteins are compared with each other and with the structures of natural TPR domains. Also, the unusual and perhaps unique crystal-packing interactions resulting in pseudo-infinite crystalline superhelices observed in the different crystal forms of CTPR8 and CTPR20 are discussed. Finally, it is shown that the thermodynamic behavior of CTPR8 and CTPR20 can be predicted from the behavior of other TPRs in this series using an Ising model-based analysis. The designed protein series CTPR2-CTPR20 covers the natural size repertoire of TPR domains and as such is an excellent model system for natural TPR proteins. PubMed: 17582171DOI: 10.1107/S0907444907024353 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.3 Å) |
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