NMR analysis of type III antifreeze protein intramolecular dimer. Structural basis for enhanced activity.
J Biol Chem
; 276(2): 1304-10, 2001 Jan 12.
Article
en En
| MEDLINE
| ID: mdl-11010977
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.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas Anticongelantes Tipo III
Límite:
Animals
Idioma:
En
Revista:
J Biol Chem
Año:
2001
Tipo del documento:
Article
País de afiliación:
Japón
Pais de publicación:
Estados Unidos