4UWW

Crystallographic Structure of the Intramineral Protein Struthicalcin from Struthio camelus Eggshell

4UWW の概要

• エントリーDOI: 10.2210/pdb4uww/pdb
• 分子名称: STRUTHIOCALCIN-1 (2 entities in total)
• 機能のキーワード: structural protein
• 由来する生物種: STRUTHIO CAMELUS (AFRICAN OSTRICH)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix : P83514
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15377.08

構造登録者

Ruiz, R.R.,Moreno, A.,Romero, A. (登録日: 2014-08-14, 公開日: 2015-04-08, 最終更新日: 2024-10-23)

主引用文献

Ruiz-Arellano, R.R.,Medrano, F.J.,Moreno, A.,Romero, A.
Crystal Structure of Struthiocalcin-1, an Intramineral Protein from Struthio Camelus Eggshell, in Two Different Crystal Forms.
Acta Crystallogr.,Sect.D, 71:809-, 2015

PubMed Abstract: Biomineralization is the process by which living organisms produce minerals. One remarkable example is the formation of eggshells in birds. Struthiocalcins present in the ostrich (Struthio camellus) eggshell matrix act as biosensors of calcite growth during eggshell formation. Here, the crystal structure of struthiocalcin-1 (SCA-1) is reported in two different crystal forms. The structure is a compact single domain with an α/β fold characteristic of the C-type lectin family. In contrast to the related avian ovocleidin OC17, the electrostatic potential on the molecular surface is dominated by an acidic patch. Scanning electron microscopy combined with Raman spectroscopy indicates that these intramineral proteins (SCA-1 and SCA-2) induce calcium carbonate precipitation, leading to the formation of a stable form of calcite in the mature eggshell. Finally, the implications of these two intramineral proteins SCA-1 and SCA-2 in the nucleation of calcite during the formation of eggshells in ratite birds are discussed.

PubMed: 25849392
DOI: 10.1107/S139900471500125X

実験手法

X-RAY DIFFRACTION (1.44 Å)