4IAU

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

4IAU の概要

• エントリーDOI: 10.2210/pdb4iau/pdb
• 分子名称: Beta-gamma-crystallin, CALCIUM ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: greek key strand motif, unknown function
• 由来する生物種: Geodia cydonium (Sponge)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18526.01

構造登録者

Vergara, A.,Grassi, M.,Sica, F.,Mazzarella, L.,Merlino, A. (登録日: 2012-12-07, 公開日: 2013-06-05, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (0.99 Å)