3QAV

Crystal structure of a glutathione S-transferase from Antarctic clam Laternula elliptica

3QAV の概要

• エントリーDOI: 10.2210/pdb3qav/pdb
• 関連するPDBエントリー: 3QAW
• 分子名称: Rho-class glutathione S-transferase (2 entities in total)
• 機能のキーワード: cytosol, transferase
• 由来する生物種: Laternula elliptica
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27981.18

構造登録者

Park, A.K.,Moon, J.H.,Chi, Y.M. (登録日: 2011-01-12, 公開日: 2012-02-01, 最終更新日: 2024-03-20)

主引用文献

Park, A.K.,Moon, J.H.,Jang, E.H.,Park, H.,Ahn, I.Y.,Lee, K.S.,Chi, Y.M.
The structure of a shellfish specific GST class glutathione S-transferase from antarctic bivalve Laternula elliptica reveals novel active site architecture.
Proteins, 81:531-537, 2013

PubMed Abstract: Glutathione-S-transferases have been identified in all the living species examined so far, yet little is known about their function in marine organisms. In a previous report, the recently identified GST from Antarctic bivalve Laternula elliptica (LeGST) was classified into the rho class GST, but there are several unique features of LeGST that may justify reclassification, which could represent specific shellfish GSTs. Here, we determined the crystal structure of LeGST, which is a shellfish specific class of GST. The structural analysis showed that the relatively open and wide hydrophobic H-site of the LeGST allows this GST to accommodate various substrates. These results suggest that the H-site of LeGST may be the result of adaptation to their environments as sedentary organisms.

PubMed: 23152139
DOI: 10.1002/prot.24208

実験手法

X-RAY DIFFRACTION (2.1 Å)