1C89

NMR STRUCTURE OF INTRAMOLECULAR DIMER ANTIFREEZE PROTEIN RD3, 40 SA STRUCTURES

1C89 の概要

• エントリーDOI: 10.2210/pdb1c89/pdb
• 関連するPDBエントリー: 1C8A
• 分子名称: ANTIFREEZE PROTEIN TYPE III (1 entity in total)
• 機能のキーワード: antifreeze, thermal hysteresis protein, ice binding protein, antifreeze protein
• 由来する生物種: Pachycara brachycephalum
• 細胞内の位置: Secreted: P35753
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14490.03

構造登録者

Miura, K.,Tsuda, S. (登録日: 2000-05-04, 公開日: 2001-02-28, 最終更新日: 2023-12-27)

主引用文献

Miura, K.,Ohgiya, S.,Hoshino, T.,Nemoto, N.,Suetake, T.,Miura, A.,Spyracopoulos, L.,Kondo, H.,Tsuda, S.
NMR analysis of type III antifreeze protein intramolecular dimer. Structural basis for enhanced activity.
J.Biol.Chem., 276:1304-1310, 2001

PubMed Abstract: The structure of a new antifreeze protein (AFP) variant, RD3, from antarctic eel pout (Rhigophila dearborni) with enhanced activity has been determined for the first time by nuclear magnetic resonance spectroscopy. RD3 comprises a unique translational topology of two homologous type III AFP globular domains, each containing one flat, ice binding plane. The ice binding plane of the N domain is located approximately 3.5 A "behind" that of the C domain. The two ice binding planes are located laterally with an angle of 32 +/- 12 degrees between the planes. These results suggest that the C domain plane of RD3 binds first to the ice [1010] prism plane in the <0001> direction, which induces successive ice binding of the N domain in the <0101> direction. This manner of ice binding caused by the unique structural topology of RD3 is thought to be crucial for the significant enhancement of antifreeze activity, especially at low AFP concentrations.

PubMed: 11010977
DOI: 10.1074/jbc.M007902200

実験手法

SOLUTION NMR