1qk4
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TOXOPLASMA GONDII HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE IMP COMPLEX
OverviewOverview
The crystal structures of the guanosine 5'-monophosphate (GMP) and inosine, 5'-monophosphate (IMP) complexes of Toxoplasma gondii hypoxanthine-guanine, phosphoribosyltransferase (HGPRT) have been determined at 1.65 and 1.90 A, resolution. These complexes, which crystallize in space groups P2(1) (a =, 65.45 A, b = 90.84 A, c = 80. 26 A, and beta = 92.53 degrees ) and, P2(1)2(1)2(1) (a = 84.54 A, b = 102.44 A, and c = 108.83 A), each comprise, a tetramer in the crystallographic asymmetric unit. All active sites in, the tetramers are fully occupied by the nucleotide. Comparison of these, structures with that of the xanthosine 5'-monophosphate, (XMP)-pyrophosphate-Mg(2+) ternary complex reported in the following, article [Heroux, A., et al. (1999) Biochemistry 38, 14495-14506] shows how, T. gondii HGPRT is able to recognize guanine, hypoxanthine, and xanthine, as substrates, and suggests why the human enzyme cannot use xanthine, efficiently. Comparison with the apoenzyme reveals the structural changes, that occur upon binding of purines and ribose 5'-phosphate to HGPRT. Two, structural features important to the HGPRT mechanism, a previously, unrecognized active site loop (loop III', residues 180-184) and an active, site peptide bond (Leu78-Lys79) that adopts both the cis and the trans, configurations, are presented.
About this StructureAbout this Structure
1QK4 is a Single protein structure of sequence from Toxoplasma gondii with IMP as ligand. Active as Hypoxanthine phosphoribosyltransferase, with EC number 2.4.2.8 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of the Toxoplasma gondii hypoxanthine-guanine phosphoribosyltransferase-GMP and -IMP complexes: comparison of purine binding interactions with the XMP complex., Heroux A, White EL, Ross LJ, Borhani DW, Biochemistry. 1999 Nov 2;38(44):14485-94. PMID:10545170
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