6EIO

Crystal structure of an ice binding protein from an Antarctic Biological Consortium

6EIO の概要

• エントリーDOI: 10.2210/pdb6eio/pdb
• 分子名称: Antifreeze protein, GLYCEROL, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: antifreeze, ice-binding, antifreeze protein
• 由来する生物種: uncultured bacterium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24662.34

構造登録者

Nardini, M.,Mangiagalli, M.,Nardone, V.,Bar Dolev, M.,Vena, V.F.,Sarusi, G.,Braslavsky, I.,Lotti, M. (登録日: 2017-09-19, 公開日: 2018-03-28, 最終更新日: 2024-01-17)

主引用文献

Mangiagalli, M.,Sarusi, G.,Kaleda, A.,Bar Dolev, M.,Nardone, V.,Vena, V.F.,Braslavsky, I.,Lotti, M.,Nardini, M.
Structure of a bacterial ice binding protein with two faces of interaction with ice.
FEBS J., 285:1653-1666, 2018

PubMed Abstract: Ice-binding proteins (IBPs) contribute to the survival of many living beings at subzero temperature by controlling the formation and growth of ice crystals. This work investigates the structural basis of the ice-binding properties of EfcIBP, obtained from Antarctic bacteria. EfcIBP is endowed with a unique combination of thermal hysteresis and ice recrystallization inhibition activity. The three-dimensional structure, solved at 0.84 Å resolution, shows that EfcIBP belongs to the IBP-1 fold family, and is organized in a right-handed β-solenoid with a triangular cross-section that forms three protein surfaces, named A, B, and C faces. However, EfcIBP diverges from other IBP-1 fold proteins in relevant structural features including the lack of a 'capping' region on top of the β-solenoid, and in the sequence and organization of the regions exposed to ice that, in EfcIBP, reveal the presence of threonine-rich ice-binding motifs. Docking experiments and site-directed mutagenesis pinpoint that EfcIBP binds ice crystals not only via its B face, as common to other IBPs, but also via ice-binding sites on the C face.

PubMed: 29533528
DOI: 10.1111/febs.14434

実験手法

X-RAY DIFFRACTION (0.84 Å)