3M1X

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

Summary for 3M1X

• Entry DOI: 10.2210/pdb3m1x/pdb
• Related: 3M4S
• Descriptor: putative Endoribonuclease L-PSP, CITRATE ANION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: structural genomics, seattle structural genomics center for infectious disease, ssgcid, unknown function
• Biological source: Entamoeba histolytica
• Total number of polymer chains: 1
• Total formula weight: 15881.53

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2010-03-05, release date: 2010-03-31, Last modification date: 2025-12-24)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.2 Å)