Solution structure of the Apo C-terminal domain of the Lethocerus F1 troponin C isoform.

Biochemistry
Gian Felice de NicolaA Pastore

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. The...Continue Reading

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Citations

Jan 22, 2011·Biochemistry·Stephen R MartinAnnalisa Pastore
Dec 1, 2019·The FEBS Journal·Elisa Millana FañanásAndrea Mattevi
Jul 12, 2019·Journal of Muscle Research and Cell Motility·Belinda Bullard, Annalisa Pastore
Nov 23, 2011·Journal of Muscle Research and Cell Motility·Belinda Bullard, Annalisa Pastore

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Methods Mentioned

BETA
circular
nuclear magnetic resonance
PCR
chemical exchange
NMR
X-ray

Software Mentioned

NMRDraw
interhlx
Tensor2
Aria
NMRPipe
DaliLite
XEASY

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