Structure of native oligomeric Sprouty2 by electron microscopy and its property of electroconductivity
- Institute of Molecular and Genomic Medicine, National Health Research Institutes, Miaoli 35053, Taiwan, ROC (China)
- Institute of Molecular Biology, Academia Sinica, Taipei 11529, Taiwan, ROC (China)
- Biomedical Engineering Research Laboratories, Industrial Technology Research Institute, Hsinchu 31040, Taiwan, ROC (China)
Highlights: •Spry2 self-assembles into distinct oligomeric forms. •Self-interaction of Spry2 is detected with a high kinetic affinity in vitro. •The 3D structure of oligomeric Spry2 likes as a donut shape with two lip-cover parts. •Spry2 contains silicon and iron. •Spry2 has a potential to serve as a biological material conductor. -- Abstract: Receptor tyrosine kinases (RTKs) regulate many cellular processes, and Sprouty2 (Spry2) is known as an important regulator of RTK signaling pathways. Therefore, it is worth investigating the properties of Spry2 in more detail. In this study, we found that Spry2 is able to self-assemble into oligomers with a high-affinity KD value of approximately 16 nM, as determined through BIAcore surface plasmon resonance analysis. The three-dimensional (3D) structure of Spry2 was resolved using an electron microscopy (EM) single-particle reconstruction approach, which revealed that Spry2 is donut-shaped with two lip-cover domains. Furthermore, the method of energy dispersive spectrum obtained through EM was analyzed to determine the elements carried by Spry2, and the results demonstrated that Spry2 is a silicon- and iron-containing protein. The silicon may contribute to the electroconductivity of Spry2, and this property exhibits a concentration-dependent feature. This study provides the first report of a silicon- and iron-containing protein, and its 3D structure may allow us (1) to study the potential mechanism through the signal transduction is controlled by switching the electronic transfer on or off and (2) to develop a new type of conductor or even semiconductor using biological or half-biological hybrid materials in the future.
- OSTI ID:
- 22242112
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 439, Issue 3; Other Information: Copyright (c) 2013 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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