Crystallization of Pearl Biomineralization Protein in Microgravity Environments

DOI:10.15011//jasma.36.360105
Int. J. Microgravity Sci. Appl. 2019p360105
Author
S. NAKAE, M. SHIONYU, T. OGAWA and T. SHIRAI
Organization
Department of Bioscience, Nagahama Institute of Bio-Science and Technology, Department of Biomolecular Science, Graduate School of Life Sciences, Tohoku University
Abstract
The isoforms of jacalin-related lectins of Pteria penguin PPL3 are known to regulate biomineralization of pearl shell, although the molecular mechanisms are largely unknown. The PPL3 crystal structures were determined partly by utilizing microgravity environments on the International Space Station for three isoforms, namely, PPL3A, PPL3B, and PPL3C. The crystals grown in microgravity environments tended to diffract to higher resolutions. The crystal structures revealed the structure stabilization mechanism of PPL3 isoforms through disulfide bond formations. Also the crystal structures, in combination with docking simulations to calcite, suggested a regulatory mechanism of biomineralization by carbohydrate-binding to the PPL3 isoforms. Additionally, the N-terminal residues of PPL3 isoforms were found in pyroglutamate form in the high-resolution electron densities, which was partly explained by the post-translational modification implied from the discrepancy between amino acid and gene sequences of PPL3 isoforms.
Keyword(s)
Protein, Lectin; Biomineralization, Post-translational modification
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Received 22 October 2018, Accepted 8 January 2019, Published 31 January 2019

© The Japan Society of Microgravity Applicaiton

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