4IAU

Atomic resolution structure of Geodin, a beta-gamma crystallin from Geodia cydonium

Summary for 4IAU

• Entry DOI: 10.2210/pdb4iau/pdb
• Descriptor: Beta-gamma-crystallin, CALCIUM ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: greek key strand motif, unknown function
• Biological source: Geodia cydonium (Sponge)
• Total number of polymer chains: 1
• Total formula weight: 18526.01

Authors

Vergara, A.,Grassi, M.,Sica, F.,Mazzarella, L.,Merlino, A. (deposition date: 2012-12-07, release date: 2013-06-05, Last modification date: 2024-10-16)

Primary citation

Vergara, A.,Grassi, M.,Sica, F.,Pizzo, E.,D'Alessio, G.,Mazzarella, L.,Merlino, A.
A novel interdomain interface in crystallins: structural characterization of the [beta][gamma]-crystallin from Geodia cydonium at 0.99 A resolution
Acta Crystallogr.,Sect.D, 69:960-967, 2013

PubMed Abstract: 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 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.

PubMed: 23695240
DOI: 10.1107/S0907444913003569

Experimental method

X-RAY DIFFRACTION (0.99 Å)