Structures of a histidine triad family protein from Entamoeba histolytica bound to sulfate AMP and GMP

摘要

Three structures of the histidine triad family protein from Entamoeba histolytica, the causative agent of amoebic dysentery, were solved at high resolution within the Seattle Structural Genomics Center for Infectious Disease (SSGCID). The structures have sulfate (PDB entry ), AMP (PDB entry ) or GMP (PDB entry ) bound in the active site, with sulfate occupying the same space as the α-phosphate of the two nucleotides. The C^α backbones of the three structures are nearly superimposable, with pairwise r.m.s.d.s ranging from 0.06 to 0.13 Å.