1bd3

<StructureSection load='1bd3' size='340' side='right' caption='[[1bd3]], [[Resolution|resolution]] 1.93&Aring;' scene=''>

<table><tr><td colspan='2'>[[1bd3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Toxgo Toxgo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BD3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BD3 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Uracil_phosphoribosyltransferase Uracil phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.9 2.4.2.9] </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=1bd3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bd3 OCA], [http://pdbe.org/1bd3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bd3 RCSB], [http://www.ebi.ac.uk/pdbsum/1bd3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bd3 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/UPP_TOXGO UPP_TOXGO]] Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.<ref>PMID:9247925</ref>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bd/1bd3_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

Uracil phosphoribosyltransferase (UPRTase) catalyzes the transfer of a ribosyl phosphate group from alpha-D-5-phosphoribosyl-1-pyrophosphate to the N1 nitrogen of uracil. The UPRTase from the opportunistic pathogen Toxoplasma gondii is a rational target for antiparasitic drug design. To aid in structure-based drug design studies against toxoplasmosis, the crystal structures of the T.gondii apo UPRTase (1.93 A resolution), the UPRTase bound to its substrate, uracil (2.2 A resolution), its product, UMP (2.5 A resolution), and the prodrug, 5-fluorouracil (2.3 A resolution), have been determined. These structures reveal that UPRTase recognizes uracil through polypeptide backbone hydrogen bonds to the uracil exocyclic O2 and endocyclic N3 atoms and a backbone-water-exocyclic O4 oxygen hydrogen bond. This stereochemical arrangement and the architecture of the uracil-binding pocket reveal why cytosine and pyrimidines with exocyclic substituents at ring position 5 larger than fluorine, including thymine, cannot bind to the enzyme. Strikingly, the T. gondii UPRTase contains a 22 residue insertion within the conserved PRTase fold that forms an extended antiparallel beta-arm. Leu92, at the tip of this arm, functions to cap the active site of its dimer mate, thereby inhibiting the escape of the substrate-binding water molecule.

 

<div class="pdbe-citations 1bd3" style="background-color:#fffaf0;"></div>

[[Category: Toxgo]]

[[Category: Uracil phosphoribosyltransferase]]

[[Category: Brennan, R G]]

[[Category: Carter, D]]

[[Category: Roos, D]]

[[Category: Schumacher, M A]]

[[Category: Scott, D]]

[[Category: Ullman, B]]

[[Category: Uprtase]]