De Sanctis, Silvia and Wenzler, Michael and Kroeger, Nils and Malloni, Wilhelm M. and Sumper, Manfred and Deutzmann, Rainer and Zadravec, Patrick and Brunner, Eike and Kremer, Werner and Kalbitzer, Hans Robert (2016) PSCD Domains of Pleuralin-1 from the Diatom Cylindrotheca fusiformis: NMR Structures and Interactions with Other Biosilica-Associated Proteins. STRUCTURE, 24 (7). pp. 1178-1191. ISSN 0969-2126, 1878-4186
Full text not available from this repository. (Request a copy)Abstract
Diatoms are eukaryotic unicellular algae characterized by silica cell walls and associated with three unique protein families, the pleuralins, frustulins, and silaffins. The NMR structure of the PSCD4 domain of pleuralin-1 from Cylindrotheca fusiformis contains only three short helical elements and is stabilized by five unique disulfide bridges. PSCD4 contains two binding sites for Ca2+ ions with millimolar affinity. NMR-based interaction studies show an interaction of the domain with native silaffin-1A as well as with alpha-frustulins. The interaction sites of the two proteins mapped on the PSCD4 structure are contiguous and show only a small overlap. A plausible functional role of pleuralin could be to bind simultaneously silaffin-1A located inside the cell wall and alpha-frustulin coating the cell wall, thus connecting the interfaces between hypotheca and epitheca at the girdle bands. Restrained molecular dynamics calculations suggest a bead-chain-like structure of the central part of pleuralin-1.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | CHEMICAL-SHIFT; CELL-WALL; ORIENTED MACROMOLECULES; SECONDARY STRUCTURE; AMINO-ACID; ASSIGNMENT; PEPTIDES; C-13; SPECTROSCOPY; COMBINATION; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 02 Apr 2019 11:59 |
| Last Modified: | 02 Apr 2019 11:59 |
| URI: | https://pred.uni-regensburg.de/id/eprint/3640 |
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