Crystallization and preliminary X-ray analysis of the Ca{sup 2+}-bound C-terminal lobe of troponin C in complex with a troponin I-derived peptide fragment from Akazara scallop
- Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, Bunkyo-ku, Tokyo 113-8657 (Japan)
- Laboratory of Biochemistry and Biotechnology, Graduate School of Fisheries Sciences, Hokkaido University, Hakodate, Hokkaido 041-8611 (Japan)
- Department of Physiology II, The Jikei University School of Medicine, 3-19-18 Nishi-shinbashi, Minato-ku, Tokyo 105-8461 (Japan)
Recombinant TnC was expressed in Escherichia coli, purified, complexed with a 24-residue synthetic peptide derived from scallop troponin I (TnI) and crystallized. Troponin C (TnC) is the Ca{sup 2+}-binding component of troponin and triggers muscle contraction. TnC of the invertebrate Akazara scallop can bind only one Ca{sup 2+} at the C-terminal EF-hand motif. Recombinant TnC was expressed in Escherichia coli, purified, complexed with a 24-residue synthetic peptide derived from scallop troponin I (TnI) and crystallized. The crystals diffracted X-rays to 1.80 Å resolution and belonged to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 32.1, b = 42.2, c = 60.0 Å. The asymmetric unit was assumed to contain one molecular complex of the Akazara scallop TnC C-lobe and TnI fragment, with a Matthews coefficient of 1.83 Å{sup 3} Da{sup −1} and a solvent content of 33.0%.
- OSTI ID:
- 22360337
- Journal Information:
- Acta Crystallographica. Section F, Vol. 63, Issue Pt 6; Other Information: PMCID: PMC2335068; PMID: 17554181; PUBLISHER-ID: bo5017; OAI: oai:pubmedcentral.nih.gov:2335068; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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