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


ABSTRACT: 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 ?-phosphate of the two nucleotides. The C(?) backbones of the three structures are nearly superimposable, with pairwise r.m.s.d.s ranging from 0.06 to 0.13 Å.

SUBMITTER: Lorimer DD 

PROVIDER: S-EPMC4427167 | biostudies-literature | 2015 May

REPOSITORIES: biostudies-literature

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

Lorimer Donald D DD   Choi Ryan R   Abramov Ariel A   Nakazawa Hewitt Stephen S   Gardberg Anna S AS   Van Voorhis Wesley C WC   Staker Bart L BL   Myler Peter J PJ   Edwards Thomas E TE  

Acta crystallographica. Section F, Structural biology communications 20150421 Pt 5


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 superimposabl  ...[more]

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