دورية أكاديمية
Structures of jacalin-related lectin PPL3 regulating pearl shell biomineralization.
| العنوان: | Structures of jacalin-related lectin PPL3 regulating pearl shell biomineralization. |
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| المؤلفون: | Nakae S; Faculty of Bioscience, Nagahama Institute of Bio-Science and Technology, 1266 Tamura-Cho, Nagahama, Shiga 526-0829, Japan., Shionyu M; Faculty of Bioscience, Nagahama Institute of Bio-Science and Technology, 1266 Tamura-Cho, Nagahama, Shiga 526-0829, Japan., Ogawa T; Department of Biomolecular Science, Graduate School of Life Sciences, Tohoku University, Sendai, Miyagi 980-8577, Japan., Shirai T; Faculty of Bioscience, Nagahama Institute of Bio-Science and Technology, 1266 Tamura-Cho, Nagahama, Shiga 526-0829, Japan. |
| المصدر: | Proteins [Proteins] 2018 Jun; Vol. 86 (6), pp. 644-653. Date of Electronic Publication: 2018 Mar 23. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Wiley-Liss Country of Publication: United States NLM ID: 8700181 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1097-0134 (Electronic) Linking ISSN: 08873585 NLM ISO Abbreviation: Proteins Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: New York, NY : Wiley-Liss Original Publication: New York : Alan R. Liss, c1986- |
| مواضيع طبية MeSH: | Biomineralization*, Lectins/*chemistry , Pinctada/*chemistry , Plant Lectins/*chemistry, Amino Acid Sequence ; Amino Acids/chemistry ; Animals ; Binding Sites ; Calcium Carbonate/chemistry ; Carbohydrates/chemistry ; Molecular Docking Simulation ; Phylogeny ; Protein Binding ; Protein Conformation, beta-Strand ; Protein Isoforms/chemistry |
| مستخلص: | The nacreous layer of pearl oysters is one of the major biominerals of commercial and industrial interest. Jacalin-related lectins, including PPL3 isoforms, are known to regulate biomineralization of the Pteria penguin pearl shell, although the molecular mechanisms are largely unknown. The PPL3 crystal structures were determined partly by utilizing microgravity environments for 3 isoforms, namely, PPL3A, PPL3B, and PPL3C. The structures revealed a tail-to-tail dimer structure established by forming a unique inter-subunit disulfide bond at C-termini. The N-terminal residues were found in pyroglutamate form, and this was partly explained by the post-translational modification of PPL3 isoforms implied from the discrepancy between amino acid and gene sequences. The complex structures with trehalose and isomaltose indicated that the novel specificity originated from the unique α-helix of PPL3 isoforms. Docking simulations of PPL3B to various calcite crystal faces suggested the edge of a β-sheet and the carbohydrate-binding site rich in charged residues were the interface to the biomineral, and implied that the isoforms differed in calcite interactions. (© 2018 Wiley Periodicals, Inc.) |
| فهرسة مساهمة: | Keywords: biomineralization; calcite; docking simulation; lectin; post-translational modification |
| المشرفين على المادة: | 0 (Amino Acids) 0 (Carbohydrates) 0 (Lectins) 0 (Plant Lectins) 0 (Protein Isoforms) 0 (jacalin) H0G9379FGK (Calcium Carbonate) |
| تواريخ الأحداث: | Date Created: 20180311 Date Completed: 20191002 Latest Revision: 20191002 |
| رمز التحديث: | 20231215 |
| DOI: | 10.1002/prot.25491 |
| PMID: | 29524263 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1097-0134 |
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| DOI: | 10.1002/prot.25491 |