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Default Solution NMR Structures of the C-domain of Tetrahymena Cytoskeletal Protein Tcb2 Reveal Distinct Calcium-Induced Structural Rearrangements.

Solution NMR Structures of the C-domain of Tetrahymena Cytoskeletal Protein Tcb2 Reveal Distinct Calcium-Induced Structural Rearrangements.

Related Articles Solution NMR Structures of the C-domain of Tetrahymena Cytoskeletal Protein Tcb2 Reveal Distinct Calcium-Induced Structural Rearrangements.

Proteins. 2016 Aug 2;

Authors: Kilpatrick AM, Honts JE, Sleister HM, Fowler CA

Abstract
Tcb2 is a calcium-binding protein that localizes to the membrane-associated skeleton of the ciliated protozoan Tetrahymena thermophila with hypothesized roles in ciliary movement, cell cortex signaling, and pronuclear exchange. Tcb2 has also been implicated in a unique calcium-triggered, ATP-independent type of contractility exhibited by filamentous networks isolated from the Tetrahymena cytoskeleton. To gain insight into Tcb2's structure-function relationship and contractile properties, we determined solution NMR structures of its C-terminal domain in the calcium-free and calcium-bound states. The overall architecture is similar to other calcium-binding proteins, with paired EF-hand calcium-binding motifs. Comparison of the two structures reveals that Tcb2-C's calcium-induced conformational transition differs from the prototypical calcium sensor calmodulin, suggesting that the two proteins play distinct functional roles in Tetrahymena and likely have different mechanisms of target recognition. Future studies of the full-length protein and the identification of Tcb2 cellular targets will help establish the molecular basis of Tcb2 function and its unique contractile properties. This article is protected by copyright. All rights reserved.


PMID: 27488393 [PubMed - as supplied by publisher]



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