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| | <StructureSection load='1tc1' size='340' side='right'caption='[[1tc1]], [[Resolution|resolution]] 1.41Å' scene=''> | | <StructureSection load='1tc1' size='340' side='right'caption='[[1tc1]], [[Resolution|resolution]] 1.41Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1tc1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Trycr Trycr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TC1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TC1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1tc1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_cruzi Trypanosoma cruzi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TC1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TC1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMB:FORMYCIN+B'>FMB</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</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]] 1.41Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMB:FORMYCIN+B'>FMB</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></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=1tc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tc1 OCA], [http://pdbe.org/1tc1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tc1 RCSB], [http://www.ebi.ac.uk/pdbsum/1tc1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tc1 ProSAT]</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=1tc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tc1 OCA], [https://pdbe.org/1tc1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tc1 RCSB], [https://www.ebi.ac.uk/pdbsum/1tc1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tc1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q4DRC4_TRYCC Q4DRC4_TRYCC] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Hypoxanthine phosphoribosyltransferase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Trycr]] | + | [[Category: Trypanosoma cruzi]] |
| - | [[Category: Eakin, A E]] | + | [[Category: Craig III SP]] |
| - | [[Category: Fletterick, R J]] | + | [[Category: Eakin AE]] |
| - | [[Category: Focia, P J]] | + | [[Category: Fletterick RJ]] |
| - | [[Category: III, S P.Craig]] | + | [[Category: Focia PJ]] |
| - | [[Category: Nieves-Alicea, R]] | + | [[Category: Nieves-Alicea R]] |
| - | [[Category: Nucleotide metabolism]]
| + | |
| - | [[Category: Phosphoribosyltransferase]]
| + | |
| - | [[Category: Purine salvage]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q4DRC4_TRYCC
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 hypoxanthine phosphoribosyltransferase (HPRT) from Trypanosoma cruzi, etiologic agent of Chagas' disease, was cocrystallized with the inosine analogue Formycin B (FmB) and the structure determined to 1.4 A resolution. This is the highest resolution structure yet reported for a phosphoribosyltransferase (PRT), and the asymmetric unit of the crystal contains a dimer of closely associated, nearly identical subunits. A conserved nonproline cis peptide in one active-site loop exposes the main-chain nitrogen to the enzyme active site, while the adjacent lysine side chain interacts with the other subunit of the dimer, thereby providing a possible mechanism for communication between the subunits and their active sites. The three-dimensional coordinates for the invariant Ser103-Tyr104 dipeptide are reported here for the first time. These are the only highly conserved residues in a second active-site loop, termed the long flexible loop, which is predicted to close over the active site of HPRTs to protect a labile transition state [Eads et al. (1994) Cell 78, 325-334]. This structure represents a major step forward in efforts to design/discover potent selective inhibitors of the HPRT of T. cruzi.
A 1.4 A crystal structure for the hypoxanthine phosphoribosyltransferase of Trypanosoma cruzi.,Focia PJ, Craig SP 3rd, Nieves-Alicea R, Fletterick RJ, Eakin AE Biochemistry. 1998 Oct 27;37(43):15066-75. PMID:9790669[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Focia PJ, Craig SP 3rd, Nieves-Alicea R, Fletterick RJ, Eakin AE. A 1.4 A crystal structure for the hypoxanthine phosphoribosyltransferase of Trypanosoma cruzi. Biochemistry. 1998 Oct 27;37(43):15066-75. PMID:9790669 doi:10.1021/bi981052s
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