Abstract
Background: The phosphatidic acid (PtdOH) binding site of TGD4 is not yet known. Results: Amino acids 1-80 and 110-145 of TGD4 represent two PtdOH interacting sequences and TGD4 forms a homodimer in vitro and in vivo. Conclusion: TGD4 N terminus binds PtdOH while its C terminus interacts with a second TGD4 protein. Significance: This work reveals the structural functional relationship of an essential chloroplast β-barrel lipid transfer protein.© 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
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CITATION STYLE
Wang, Z., Anderson, N. S., & Benning, C. (2013). The phosphatidic acid binding site of the arabidopsis trigalactosyldiacylglycerol 4 (TGD4) protein required for lipid import into chloroplasts. Journal of Biological Chemistry, 288(7), 4763–4771. https://doi.org/10.1074/jbc.M112.438986
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