Structural highlights
Function
A0A090CRQ5_PODAN
Publication Abstract from PubMed
Linear repeat proteins often have high structural similarity and low ( approximately 25%) pairwise sequence identities (PSI) among modules. We identified a unique P. anserina (Pa) sequence with tetratricopeptide repeat (TPR) homology, which contains longer (42 residue) repeats (42PRs) with an average PSI >91%. We determined the crystal structure of five tandem Pa 42PRs to 1.6 A, and examined the stability and solution properties of constructs containing three to six Pa 42PRs. Compared with 34-residue TPRs (34PRs), Pa 42PRs have a one-turn extension of each helix, and bury more surface area. Unfolding transitions shift to higher denaturant concentration and become sharper as repeats are added. Fitted Ising models show Pa 42PRs to be more cooperative than consensus 34PRs, with increased magnitudes of intrinsic and interfacial free energies. These results demonstrate the tolerance of the TPR motif to length variation, and provide a basis to understand the effects of helix length on intrinsic/interfacial stability.
A Naturally Occurring Repeat Protein with High Internal Sequence Identity Defines a New Class of TPR-like Proteins.,Marold JD, Kavran JM, Bowman GD, Barrick D Structure. 2015 Oct 1. pii: S0969-2126(15)00369-X. doi:, 10.1016/j.str.2015.07.022. PMID:26439765[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Marold JD, Kavran JM, Bowman GD, Barrick D. A Naturally Occurring Repeat Protein with High Internal Sequence Identity Defines a New Class of TPR-like Proteins. Structure. 2015 Oct 1. pii: S0969-2126(15)00369-X. doi:, 10.1016/j.str.2015.07.022. PMID:26439765 doi:http://dx.doi.org/10.1016/j.str.2015.07.022
