Startseite Structure of the Ca2+-saturated C-terminal domain of scallop troponin C in complex with a troponin I fragment
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Structure of the Ca2+-saturated C-terminal domain of scallop troponin C in complex with a troponin I fragment

  • Yusuke S. Kato , Fumiaki Yumoto , Hiroyuki Tanaka , Takuya Miyakawa , Yumiko Miyauchi , Daijiro Takeshita , Yoriko Sawano , Takao Ojima , Iwao Ohtsuki und Masaru Tanokura EMAIL logo
Veröffentlicht/Copyright: 4. Dezember 2012
Biological Chemistry
Aus der Zeitschrift Biological Chemistry Band 394 Heft 1

Abstract

Troponin C (TnC) is the Ca2+-sensing subunit of troponin that triggers the contraction of striated muscles. In scallops, the striated muscles consume little ATP energy in sustaining strong contractile forces. The N-terminal domain of TnC works as the Ca2+ sensor in vertebrates, whereas scallop TnC uses the C-terminal domain as the Ca2+ sensor, suggesting that there are differences in the mechanism of the Ca2+-dependent regulation of muscles between invertebrates and vertebrates. Here, we report the crystal structure of Akazara scallop (Chlamys nipponensis akazara) adductor muscle TnC C-terminal domain (asTnCC) complexed with a short troponin I fragment (asTnIS) and Ca2+. The electron density of a Ca2+ ion is observed in only one of the two EF-hands. The EF-hands of asTnCC can only be in the fully open conformation with the assistance of asTnIS. The number of hydrogen bonds between asTnCC and asTnIS is markedly lower than the number in the vertebrate counterparts. The Ca2+ modulation on the binding between asTnCC and asTnIS is weaker, but structural change of the complex depending on Ca2+ concentration was observed. Together, these findings provide a detailed description of the distinct molecular mechanism of contractile regulation in the scallop adductor muscle from that of vertebrates.

Keywords: crystal structure; interaction; invertebrate; isothermal titration microcalorimetry; mollusc; muscle
Corresponding author: Masaru Tanokura, Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, Japan
Received: 2012-3-14
Accepted: 2012-7-26
Published Online: 2012-12-04
Published in Print: 2013-01-01

©2012 by Walter de Gruyter Berlin Boston

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https://doi.org/10.1515/hsz-2012-0152
Schlagwörter für diesen Artikel
crystal structure; interaction; invertebrate; isothermal titration microcalorimetry; mollusc; muscle

Artikel in diesem Heft

  1. Masthead
  2. Masthead
  3. Reviews
  4. Exosomes: the ideal nanovectors for biodelivery
  5. Biological applications of the electrochemical sensing of nitric oxide: fundamentals and recent developments
  6. Minireview
  7. Cerebral cavernous malformation is a vascular disease associated with activated RhoA signaling
  8. Research Articles/Short Communications
  9. Protein Structure and Function
  10. Diversity, abundance, and sex-specific expression of chemosensory proteins in the reproductive organs of the locust Locusta migratoria manilensis
  11. Structure of the Ca2+-saturated C-terminal domain of scallop troponin C in complex with a troponin I fragment
  12. An acetylation site in lectin domain modulates the biological activity of polypeptide GalNAc-transferase-2
  13. Reengineering of subtilisin Carlsberg for oxidative resistance
  14. New insight into the molecular switch mechanism of human Rho family proteins: shifting a paradigm
  15. Cell Biology and Signaling
  16. HbG200-mediated preinduction of heme oxygenase-1 improves bile flow and ameliorates pericentral downregulation of Bsep and Mrp2 following experimental liver ischemia and reperfusion
  17. Effect of silver nanoparticles on human primary keratinocytes
  18. Multifunctional silica nanoparticles for optical and magnetic resonance imaging
  19. Proteolysis
  20. Activation profiles of human kallikrein-related peptidases by matrix metalloproteinases
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