2AVP

Crystal structure of an 8 repeat consensus TPR superhelix

Summary for 2AVP

• Entry DOI: 10.2210/pdb2avp/pdb
• Descriptor: synthetic consensus TPR protein, CADMIUM ION (3 entities in total)
• Functional Keywords: tetratricopeptide repeat, tpr, consensus protein, superhelix, de novo protein
• Total number of polymer chains: 1
• Total formula weight: 8453.57

Authors

Kajander, T.,Cortajarena, A.L.,Main, E.R.,Mochrie, S.,Regan, L. (deposition date: 2005-08-30, release date: 2005-09-13, Last modification date: 2024-02-14)

Primary citation

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

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: 17582171
DOI: 10.1107/S0907444907024353

Experimental method

X-RAY DIFFRACTION (2.04 Å)