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| | ==TOXOPLASMA GONDII HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE IMP COMPLEX== | | ==TOXOPLASMA GONDII HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE IMP COMPLEX== |
| - | <StructureSection load='1qk4' size='340' side='right' caption='[[1qk4]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='1qk4' size='340' side='right'caption='[[1qk4]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1qk4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Toxoplasma_gondii_rh Toxoplasma gondii rh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QK4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QK4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1qk4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Toxoplasma_gondii_RH Toxoplasma gondii RH]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QK4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dbr|1dbr]], [[1hmp|1hmp]], [[1qk3|1qk3]], [[1qk5|1qk5]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hypoxanthine_phosphoribosyltransferase Hypoxanthine phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.8 2.4.2.8] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qk4 OCA], [https://pdbe.org/1qk4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qk4 RCSB], [https://www.ebi.ac.uk/pdbsum/1qk4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qk4 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qk4 OCA], [http://pdbe.org/1qk4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qk4 RCSB], [http://www.ebi.ac.uk/pdbsum/1qk4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qk4 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HGXR_TOXGO HGXR_TOXGO]] Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to the N(9) of hypoxanthine, guanine or xanthine.<ref>PMID:11188695</ref> | + | [https://www.uniprot.org/uniprot/HGXR_TOXGO HGXR_TOXGO] Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to the N(9) of hypoxanthine, guanine or xanthine.<ref>PMID:11188695</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1qk4" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1qk4" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Hypoxanthine phosphoribosyltransferase]] | + | [[Category: Large Structures]] |
| - | [[Category: Toxoplasma gondii rh]] | + | [[Category: Toxoplasma gondii RH]] |
| - | [[Category: Borhani, D W]] | + | [[Category: Borhani DW]] |
| - | [[Category: Heroux, A]] | + | [[Category: Heroux A]] |
| - | [[Category: Ross, L J]] | + | [[Category: Ross LJ]] |
| - | [[Category: White, E L]] | + | [[Category: White EL]] |
| - | [[Category: Glycosyltransferase]]
| + | |
| - | [[Category: Purine salvage]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
HGXR_TOXGO Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to the N(9) of hypoxanthine, guanine or xanthine.[1]
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 PubMed
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.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Heroux A, White EL, Ross LJ, Kuzin AP, Borhani DW. Substrate deformation in a hypoxanthine-guanine phosphoribosyltransferase ternary complex: the structural basis for catalysis. Structure. 2000 Dec 15;8(12):1309-18. PMID:11188695
- ↑ Heroux A, White EL, Ross LJ, Borhani DW. Crystal structures of the Toxoplasma gondii hypoxanthine-guanine phosphoribosyltransferase-GMP and -IMP complexes: comparison of purine binding interactions with the XMP complex. Biochemistry. 1999 Nov 2;38(44):14485-94. PMID:10545170
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