A Novel Interdomain Interface In Crystallins: Structural Characterization Of The Beta Gamma-Crystallin From Geodia Cydonium At 0. 99 Angstrom Resolution

The βγ-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 βγ-crystallins that constitute the vertebrate eye lens. This study reports the crystallographic structure at 0.99 14;Å resolution of the two-domain βγ-crystallin (geodin) from the sponge Geodia cydonium. This is the most ancient member of the βγ-crystallin superfamily in metazoans. The X-ray structure shows that the geodin domains adopt the typical βγ-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. © 2013 International Union of Crystallography.

A Novel Interdomain Interface In Crystallins: Structural Characterization Of The Beta Gamma-Crystallin From Geodia Cydonium At 0. 99 Angstrom Resolution

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