2MK0

Structure of the PSCD4-domain of the cell wall protein pleuralin-1 from the diatom Cylindrotheca fusiformis

2MK0 の概要

• エントリーDOI: 10.2210/pdb2mk0/pdb
• 分子名称: HEP200 protein (1 entity in total)
• 機能のキーワード: diatom cell wall protein, pleuralin-1, pscd4-domain, cell surface/cell wall, structural protein
• 由来する生物種: Cylindrotheca fusiformis (Marine diatom)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12766.32

構造登録者

De Sanctis, S.,Wenzler, M.,Kroeger, N.,Malloni, W.M.,Sumper, M.,Deutzmann, R.,Zadravec, P.,Brunner, E.,Kremer, W.,Kalbitzer, S.H.R. (登録日: 2014-01-22, 公開日: 2015-02-25, 最終更新日: 2024-11-06)

主引用文献

De Sanctis, S.,Wenzler, M.,Kroger, N.,Malloni, W.M.,Sumper, M.,Deutzmann, R.,Zadravec, P.,Brunner, E.,Kremer, W.,Kalbitzer, H.R.
PSCD Domains of Pleuralin-1 from the Diatom Cylindrotheca fusiformis: NMR Structures and Interactions with Other Biosilica-Associated Proteins.
Structure, 24:1178-1191, 2016

PubMed 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 Ca(2+) ions with millimolar affinity. NMR-based interaction studies show an interaction of the domain with native silaffin-1A as well as with α-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 α-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.

PubMed: 27320836
DOI: 10.1016/j.str.2016.04.021

実験手法

SOLUTION NMR