5XNA

Crystal structure of a secretary abundant heat soluble (SAHS) protein from Ramazzottius varieornatus (from dimer sample)

5XNA の概要

• エントリーDOI: 10.2210/pdb5xna/pdb
• 分子名称: SAHS1, ZINC ION, MAGNESIUM ION, ... (8 entities in total)
• 機能のキーワード: secretary abundant heat soluble protein, ramazzottius varieornatus, fatty acid binding protein, lipid transport
• 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: 33952.87

構造登録者

Fukuda, Y.,Miura, Y.,Mizohata, E.,Inoue, T. (登録日: 2017-05-19, 公開日: 2017-07-26, 最終更新日: 2024-03-27)

主引用文献

Fukuda, Y.,Miura, Y.,Mizohata, E.,Inoue, T.
Structural insights into a secretory abundant heat-soluble protein from an anhydrobiotic tardigrade, Ramazzottius varieornatus
FEBS Lett., 591:2458-2469, 2017

PubMed Abstract: Upon stopping metabolic processes, some tardigrades can undergo anhydrobiosis. Secretory abundant heat-soluble (SAHS) proteins have been reported as candidates for anhydrobiosis-related proteins in tardigrades, which seem to protect extracellular components and/or secretory organelles. We determined structures of a SAHS protein from Ramazzottius varieornatus (RvSAHS1), which is one of the toughest tardigrades. RvSAHS1 shows a β-barrel structure similar to fatty acid-binding proteins (FABPs), in which hydrophilic residues form peculiar hydrogen bond networks, which would provide RvSAHS1 with better tolerance against dehydration. We identified two putative ligand-binding sites: one that superimposes on those of some FABPs and the other, unique to and conserved in SAHS proteins. These results indicate that SAHS proteins constitute a new FABP family.

PubMed: 28703282
DOI: 10.1002/1873-3468.12752

実験手法

X-RAY DIFFRACTION (1.802 Å)