2NCP
NMR solution structure for the C-terminal domain of Tetrahymena Tcb2 in the presence of calcium
Summary for 2NCP
| Entry DOI | 10.2210/pdb2ncp/pdb |
| Related | 2NCO |
| NMR Information | BMRB: 26724 |
| Descriptor | 25 kDa calcium-binding protein (1 entity in total) |
| Functional Keywords | calcium binding protein, ef hand, contractility, helical packing, cytoskeleton, tcb25, metal binding protein |
| Biological source | Tetrahymena thermophila |
| Total number of polymer chains | 1 |
| Total formula weight | 11578.02 |
| Authors | Fowler, A.,Kilpatrick, A.M. (deposition date: 2016-04-11, release date: 2016-08-17, Last modification date: 2024-05-15) |
| Primary citation | Kilpatrick, A.M.,Honts, J.E.,Sleister, H.M.,Fowler, C.A. Solution NMR structures of the C-domain of Tetrahymena cytoskeletal protein Tcb2 reveal distinct calcium-induced structural rearrangements. Proteins, 84:1748-1756, 2016 Cited by PubMed 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. Proteins 2016; 84:1748-1756. © 2016 Wiley Periodicals, Inc. PubMed: 27488393DOI: 10.1002/prot.25111 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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