3oxk | pdb_00003oxk
Crystal structure of a histidine triad family protein from Entamoeba histolytica, bound to GMP
Structural highlights
FunctionHIT_ENTH1 Hydrolyzes purine nucleotide phosphoramidates with a single phosphate group, including adenosine 5'monophosphoramidate (AMP-NH2), adenosine 5'monophosphomorpholidate (AMP-morpholidate) and guanosine 5'monophosphomorpholidate (GMP-morpholidate). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) generated by lysine tRNA ligase, as well as Met-AMP, His-AMP and Asp-AMP, lysyl-GMP (GMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) and AMP-N-alanine methyl ester. May also function as scaffolding protein that mediates protein-protein interactions (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThree 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 alpha-phosphate of the two nucleotides. The C(alpha) backbones of the three structures are nearly superimposable, with pairwise r.m.s.d.s ranging from 0.06 to 0.13 A. Structures of a histidine triad family protein from Entamoeba histolytica bound to sulfate, AMP and GMP.,Lorimer DD, Choi R, Abramov A, Nakazawa Hewitt S, Gardberg AS, Van Voorhis WC, Staker BL, Myler PJ, Edwards TE Acta Crystallogr F Struct Biol Commun. 2015 May;71(Pt 5):572-6. doi:, 10.1107/S2053230X1500237X. Epub 2015 Apr 21. PMID:25945711[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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