skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: 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

Abstract

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%.

Authors:
 [1];  [2]; ;  [1]; ; ;  [3];  [4];  [1]
  1. Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, Bunkyo-ku, Tokyo 113-8657 (Japan)
  2. (Japan)
  3. Laboratory of Biochemistry and Biotechnology, Graduate School of Fisheries Sciences, Hokkaido University, Hakodate, Hokkaido 041-8611 (Japan)
  4. Department of Physiology II, The Jikei University School of Medicine, 3-19-18 Nishi-shinbashi, Minato-ku, Tokyo 105-8461 (Japan)
Publication Date:
OSTI Identifier:
22360337
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal 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)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CONTRACTION; CRYSTALLIZATION; CRYSTALS; ESCHERICHIA COLI; RESOLUTION; SOLVENTS; SPACE GROUPS

Citation Formats

Yumoto, Fumiaki, Department of Physiology II, The Jikei University School of Medicine, 3-19-18 Nishi-shinbashi, Minato-ku, Tokyo 105-8461, Nagata, Koji, Miyauchi, Yumiko, Ojima, Takao, Tanaka, Hiroyuki, Nishita, Kiyoyoshi, Ohtsuki, Iwao, and Tanokura, Masaru, E-mail: amtanok@mail.ecc.u-tokyo.ac.jp. 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. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107024712.
Yumoto, Fumiaki, Department of Physiology II, The Jikei University School of Medicine, 3-19-18 Nishi-shinbashi, Minato-ku, Tokyo 105-8461, Nagata, Koji, Miyauchi, Yumiko, Ojima, Takao, Tanaka, Hiroyuki, Nishita, Kiyoyoshi, Ohtsuki, Iwao, & Tanokura, Masaru, E-mail: amtanok@mail.ecc.u-tokyo.ac.jp. 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. United Kingdom. doi:10.1107/S1744309107024712.
Yumoto, Fumiaki, Department of Physiology II, The Jikei University School of Medicine, 3-19-18 Nishi-shinbashi, Minato-ku, Tokyo 105-8461, Nagata, Koji, Miyauchi, Yumiko, Ojima, Takao, Tanaka, Hiroyuki, Nishita, Kiyoyoshi, Ohtsuki, Iwao, and Tanokura, Masaru, E-mail: amtanok@mail.ecc.u-tokyo.ac.jp. Fri . "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". United Kingdom. doi:10.1107/S1744309107024712.
@article{osti_22360337,
title = {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},
author = {Yumoto, Fumiaki and Department of Physiology II, The Jikei University School of Medicine, 3-19-18 Nishi-shinbashi, Minato-ku, Tokyo 105-8461 and Nagata, Koji and Miyauchi, Yumiko and Ojima, Takao and Tanaka, Hiroyuki and Nishita, Kiyoyoshi and Ohtsuki, Iwao and Tanokura, Masaru, E-mail: amtanok@mail.ecc.u-tokyo.ac.jp},
abstractNote = {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%.},
doi = {10.1107/S1744309107024712},
journal = {Acta Crystallographica. Section F},
number = Pt 6,
volume = 63,
place = {United Kingdom},
year = {Fri Jun 01 00:00:00 EDT 2007},
month = {Fri Jun 01 00:00:00 EDT 2007}
}