5OTB

Structure of caprine serum albumin in P1 space group

5OTB の概要

• エントリーDOI: 10.2210/pdb5otb/pdb
• 関連するPDBエントリー: 5ORF 5ORI 5OSW
• 分子名称: Albumin, TRIETHYLENE GLYCOL, PROLINE, ... (5 entities in total)
• 機能のキーワード: caprine serum albumin, goat serum albumin, p1, transport protein
• 由来する生物種: Capra hircus (Goat)
• 細胞内の位置: Secreted : B3VHM9
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 267580.38

構造登録者

Talaj, J.A.,Bujacz, A.,Bujacz, G. (登録日: 2017-08-21, 公開日: 2017-11-08, 最終更新日: 2024-10-23)

主引用文献

Bujacz, A.,Talaj, J.A.,Zielinski, K.,Pietrzyk-Brzezinska, A.J.,Neumann, P.
Crystal structures of serum albumins from domesticated ruminants and their complexes with 3,5-diiodosalicylic acid.
Acta Crystallogr D Struct Biol, 73:896-909, 2017

PubMed Abstract: Serum albumin (SA) is the most abundant protein in plasma and is the main transporter of molecules in the circulatory system of all vertebrates, with applications in medicine, the pharmaceutical industry and molecular biology. It is known that albumins from different organisms vary in sequence; thus, it is important to know the impact of the amino-acid sequence on the three-dimensional structure and ligand-binding properties. Here, crystal structures of ovine (OSA) and caprine (CSA) serum albumins, isolated from sheep and goat blood, are described, as well those of their complexes with 3,5-diiodosalicylic acid (DIS): OSA-DIS (2.20 Å resolution) and CSA-DIS (1.78 Å resolution). The ligand-free OSA structure was determined in the trigonal space group P321 at 2.30 Å resolution, while that of CSA in the orthorhombic space group P222 was determined at 1.94 Å resolution. Both albumins are also capable of crystallizing in the triclinic space group P1, giving isostructural crystals that diffract to around 2.5 Å resolution. A comparison of OSA and CSA with the closely related bovine serum albumin (BSA) shows both similarities and differences in the distribution of DIS binding sites. The investigated serum albumins from domesticated ruminants in their complexes with DIS are also compared with the analogous structures of equine and human serum albumins (ESA-DIS and HSA-DIS). Surprisingly, despite 98% sequence similarity, OSA binds only two molecules of DIS, whereas CSA binds six molecules of this ligand. Moreover, the binding of DIS to OSA and CSA introduced changes in the overall architecture of the proteins, causing not only different conformations of the amino-acid side chains in the binding pockets, but also a significant shift of the whole helices, changing the volume of the binding cavities.

PubMed: 29095162
DOI: 10.1107/S205979831701470X

実験手法

X-RAY DIFFRACTION (2.5 Å)