A novel interdomain interface in crystallins: structural characterization of the ßγ-crystallin from Geodia cydonium at 0.99 Å resolution.
Acta Crystallogr D Biol Crystallogr
; 69(Pt 6): 960-7, 2013 Jun.
Article
en En
| MEDLINE
| ID: mdl-23695240
ABSTRACT
The ßγ-crystallin superfamily includes highly diverse proteins belonging to all of the kingdoms of life. Based on structural topology, these proteins are considered to be evolutionarily related to the long-lived ßγ-crystallins that constitute the vertebrate eye lens. This study reports the crystallographic structure at 0.99 Å resolution of the two-domain ßγ-crystallin (geodin) from the sponge Geodia cydonium. This is the most ancient member of the ßγ-crystallin superfamily in metazoans. The X-ray structure shows that the geodin domains adopt the typical ßγ-crystallin fold with a paired Greek-key motif, thus confirming the hypothesis that the crystallin-type scaffold used in the evolution of bacteria and moulds was recruited very early in metazoans. As a significant new structural feature, the sponge protein possesses a unique interdomain interface made up by pairing between the second motif of the first domain and the first motif of the second domain. The atomic resolution also allowed a detailed analysis of the calcium-binding site of the protein.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Cristalinas
/
Geodia
Límite:
Animals
Idioma:
En
Revista:
Acta Crystallogr D Biol Crystallogr
Año:
2013
Tipo del documento:
Article
País de afiliación:
Italia