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

Donald D Lorimer, Ryan Choi, Ariel Abramov, Stephen Nakazawa Hewitt, Anna S Gardberg, Wesley C Van Voorhis, Bart L Staker, Peter J Myler, Thomas E Edwards

Acta crystallographica. Section F, Structural biology communications 2015 May

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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 3oj7), AMP (PDB entry 3omf) or GMP (PDB entry 3oxk) 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.

Citation

Donald D Lorimer, Ryan Choi, Ariel Abramov, Stephen Nakazawa Hewitt, Anna S Gardberg, Wesley C Van Voorhis, Bart L Staker, Peter J Myler, Thomas E Edwards. Structures of a histidine triad family protein from Entamoeba histolytica bound to sulfate, AMP and GMP. Acta crystallographica. Section F, Structural biology communications. 2015 May;71(Pt 5):572-6