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Crystallographic data for the 9000 dalton wheat non-specific phospholipid transfer protein
E Pebay-Peyroula1, C Cohen-Addad, M S Lehmann
1Institut Laue-Langevin, Grenoble, France.
Journal of Molecular Biology
|July 20, 1992
Summary
Wheat non-specific phospholipid transfer protein (nsLTP) has high phospholipid affinity and transfers lipids in vitro. Its in vivo function remains unknown, despite structural characterization.
Area of Science:
- Biochemistry
- Structural Biology
- Plant Science
Background:
- Wheat non-specific phospholipid transfer proteins (nsLTPs) are small proteins characterized by four disulfide bridges.
- These proteins exhibit high affinity for phospholipids and are known to facilitate phospholipid transfer in vitro.
Purpose of the Study:
- To characterize the wheat non-specific phospholipid transfer protein.
- To provide insights into its structural properties relevant to its function.
Main Methods:
- Crystallization of the wheat non-specific phospholipid transfer protein.
- X-ray diffraction analysis to determine crystal structure and resolution.
Main Results:
- The protein has a molecular weight of 9607 Da.
- Crystallization in space group P2(1) with specific unit cell parameters (a = 40.73 Å, b = 112.11 Å, c = 50.44 Å, β = 106.80°).
- The crystals diffract X-rays to 3 Å resolution, enabling structural determination.
Conclusions:
- The structural data provides a foundation for understanding the molecular mechanisms of phospholipid binding and transfer.
- Further research is needed to elucidate the in vivo function of wheat nsLTP.