3M4S

Crystal structure of a putative endoribonuclease L-PSP from Entamoeba histolytica, orthorhombic form

3M4S の概要

• エントリーDOI: 10.2210/pdb3m4s/pdb
• 関連するPDBエントリー: 3M1X
• 分子名称: putative Endoribonuclease L-PSP, CHLORIDE ION (3 entities in total)
• 機能のキーワード: structural genomics, seattle structural genomics center for infectious disease, ssgcid, unknown function
• 由来する生物種: Entamoeba histolytica
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 93881.32

構造登録者

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2010-03-11, 公開日: 2010-03-31, 最終更新日: 2025-12-24)

主引用文献

Ojuromi, O.T.,Giwa, A.O.,Gardberg, A.,Subramanian, S.,Myler, P.J.,Abendroth, J.,Staker, B.,Asojo, O.A.
Crystal structures of the putative endoribonuclease L-PSP from Entamoeba histolytica.
Acta Crystallogr.,Sect.F, 81:226-234, 2025

PubMed Abstract: Entamoeba histolytica causes amebiasis, a neglected disease that kills ∼100 000 people globally each year. Due to emerging drug resistance, E. histolytica is one of the target organisms for structure-based drug discovery by the Seattle Structural Genomics Center for Infectious Disease (SSGCID). Purification, crystallization and three structures of the putative drug target endoribonuclease L-PSP from E. histolytica (EhL-PSP) are presented. EhL-PSP has a two-layer α/β-sandwich with structural homology to endoribonuclease L-PSP. All three structures reveal the prototypical YjgF/YER057c/UK114 family trimer topology with accessible allosteric active sites. Citrate molecules from the crystallization solution are bound to the allosteric site in two of the three reported structures. The large allosteric site of EhL-PSP is well conserved with bacterial YjgF/YER057c/UK114 family members and could be targeted for inhibition, drug discovery or repurposing.

PubMed: 40314238
DOI: 10.1107/S2053230X25003875

実験手法

X-RAY DIFFRACTION (2.3 Å)