2K2A

Solution Structure of the Apo C terminal domain of Lethocerus troponin C isoform F1

Summary for 2K2A

• Entry DOI: 10.2210/pdb2k2a/pdb
• NMR Information: BMRB: 15698
• Descriptor: Troponin C (1 entity in total)
• Functional Keywords: contractile protein, calcium binding protein
• Biological source: Lethocerus indicus
• Total number of polymer chains: 1
• Total formula weight: 7849.48

Authors

De Nicola, G.F.,Kelly, G.,Bullard, B.,McCormick, J. (deposition date: 2008-03-29, release date: 2009-04-07, Last modification date: 2024-05-08)

Primary citation

De Nicola, G.F.,Martin, S.,Bullard, B.,Pastore, A.
Solution structure of the Apo C-terminal domain of the Lethocerus F1 troponin C isoform.
Biochemistry, 49:1719-1726, 2010

PubMed Abstract: Muscle contraction is activated by two distinct mechanisms. One depends on the calcium influx, and the other is calcium-independent and activated by mechanical stress. A prototypical example of stretch activation is observed in insect muscles. In Lethocerus, a model system ideally suited for studying stretch activation, the two mechanisms seem to be under the control of different isoforms of troponin C (TnC), F1 and F2, which are responsible for stretch and calcium-dependent regulation, respectively. We have previously shown that F1 TnC is a typical collapsed dumbbell EF-hand protein that accommodates one calcium ion in its fourth EF-hand. When calcium loaded, the C-terminal domain of F1 TnC is in an open conformation which allows binding to troponin I. We have determined the solution structure of the isolated F1 TnC C-terminal domain in the absence of calcium and have compared it together with its dynamical properties with those of the calcium-loaded form. The domain is folded also in the absence of calcium and is in a closed conformation. Binding of a single calcium is sufficient to induce a modest but clear closed-to-open conformational transition and releases the conformational entropy observed in the calcium-free form. These results provide the first example of a TnC domain in which the presence of only one calcium ion is sufficient to induce a closed-to-open transition and clarify the role of calcium in stretch activation.

PubMed: 20104876
DOI: 10.1021/bi902094w

Experimental method

SOLUTION NMR