5Z4G

Crystal structure of secretory abundant heat soluble protein 4 from Ramazzottius varieornatus

5Z4G の概要

• エントリーDOI: 10.2210/pdb5z4g/pdb
• 分子名称: SAHS4, ZINC ION, TETRAETHYLENE GLYCOL, ... (5 entities in total)
• 機能のキーワード: tardigrade, unknown function
• 由来する生物種: Ramazzottius varieornatus (Water bear)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 37586.99

構造登録者

Fukuda, Y.,Inoue, T. (登録日: 2018-01-11, 公開日: 2018-04-11, 最終更新日: 2023-11-22)

主引用文献

Fukuda, Y.,Inoue, T.
Crystal structure of secretory abundant heat soluble protein 4 from one of the toughest "water bears" micro-animals Ramazzottius Varieornatus
Protein Sci., 27:993-999, 2018

PubMed Abstract: Though anhydrobiotic tardigrades (micro-animals also known as water bears) possess many genes of secretory abundant heat soluble (SAHS) proteins unique to Tardigrada, their functions are unknown. A previous crystallographic study revealed that a SAHS protein (RvSAHS1) from one of the toughest tardigrades, Ramazzottius varieornatus, has a β-barrel architecture similar to fatty acid binding proteins (FABPs) and two putative ligand binding sites (LBS1 and LBS2) where fatty acids can bind. However, some SAHS proteins such as RvSAHS4 have different sets of amino acid residues at LBS1 and LBS2, implying that they prefer other ligands and have different functions. Here RvSAHS4 was crystallized and analyzed under a condition similar to that for RvSAHS1. There was no electron density corresponding to a fatty acid at LBS1 of RvSAHS4, where a putative fatty acid was observed in RvSAHS1. Instead, LBS2 of RvSAHS4, which was composed of uncharged residues, captured a putative polyethylene glycol molecule. These results suggest that RvSAHS4 mainly uses LBS2 for the binding of uncharged molecules.

PubMed: 29493034
DOI: 10.1002/pro.3393

実験手法

X-RAY DIFFRACTION (1.5 Å)