2nco

NMR solution structure for the C-terminal domain of Tetrahymena Tcb2 in the absence of calcium

spinqualitylabelsall models 2nco, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2nco is a 1 chain structure with sequence from Tetth. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2ncp Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CB25_TETTH] Expected to play a crucial role in calcium-dependent regulation of ciliary movement. Publication Abstract from PubMed 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. Proteins 2016. (c) 2016 Wiley Periodicals, Inc. Solution NMR structures of the C-domain of Tetrahymena cytoskeletal protein Tcb2 reveal distinct calcium-induced structural rearrangements.,Kilpatrick AM, Honts JE, Sleister HM, Fowler CA Proteins. 2016 Aug 2. doi: 10.1002/prot.25111. PMID:27488393 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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