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

Acta Crystallogr F Struct Biol Commun. 2015 May;71(Pt 5):572-6. doi: 10.1107/S2053230X1500237X. Epub 2015 Apr 21.

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 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.

Keywords: SSGCID; Seattle Structural Genomics Center for Infectious Disease; hydrolase; metal-binding protein; structural genomics.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Adenosine Monophosphate / metabolism*
  • Amino Acid Sequence
  • Crystallization
  • Entamoeba histolytica / chemistry*
  • Entamoeba histolytica / genetics
  • Entamoeba histolytica / metabolism
  • Guanosine Monophosphate / metabolism*
  • Hydrolases / chemistry*
  • Hydrolases / genetics
  • Hydrolases / metabolism
  • Molecular Sequence Data
  • Protein Binding / physiology
  • Protein Structure, Secondary
  • Sulfates / metabolism*

Substances

  • Sulfates
  • histidine triad protein
  • Adenosine Monophosphate
  • Guanosine Monophosphate
  • Hydrolases

Associated data

  • PDB/3OJ7
  • PDB/3OMF
  • PDB/3OXK