2NCP

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

2NCP の概要

• エントリーDOI: 10.2210/pdb2ncp/pdb
• 関連するPDBエントリー: 2NCO
• NMR情報: BMRB: 26724
• 分子名称: 25 kDa calcium-binding protein (1 entity in total)
• 機能のキーワード: calcium binding protein, ef hand, contractility, helical packing, cytoskeleton, tcb25, metal binding protein
• 由来する生物種: Tetrahymena thermophila
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11578.02

構造登録者

Fowler, A.,Kilpatrick, A.M. (登録日: 2016-04-11, 公開日: 2016-08-17, 最終更新日: 2024-05-15)

主引用文献

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

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: 27488393
DOI: 10.1002/prot.25111

実験手法

SOLUTION NMR