1dbr: Difference between revisions

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<StructureSection load='1dbr' size='340' side='right'caption='[[1dbr]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1dbr' size='340' side='right'caption='[[1dbr]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1dbr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Toxgo Toxgo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DBR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DBR FirstGlance]. <br>
<table><tr><td colspan='2'>[[1dbr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DBR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DBR FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=1dbr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dbr OCA], [https://pdbe.org/1dbr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dbr RCSB], [https://www.ebi.ac.uk/pdbsum/1dbr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dbr 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=1dbr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dbr OCA], [https://pdbe.org/1dbr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dbr RCSB], [https://www.ebi.ac.uk/pdbsum/1dbr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dbr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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>
[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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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dbr ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dbr ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Crystal structures of substrate-free and XMP-soaked hypoxanthine-guanine-xanthine phosphoribosyltransferase (HGXPRTase) of the opportunistic pathogen Toxoplasma gondii have been determined to 2.4 and 2.9 A resolution, respectively. HGXPRTase displays the conserved PRTase fold. In the structure of the enzyme bound to its product, a long flexible loop (residues 115-126) is located away from the active site. Comparison to the substrate-free structure reveals a striking relocation of the loop, which is poised to cover the catalytic pocket, thus providing a mechanism by which the HG(X)PRTases shield their oxocarbonium transition states from nucleophilic attack by the bulk solvent. The conserved Ser 117-Tyr 118 dipeptide within the loop is brought to the active site, completing the ensemble of catalytic residues.
Crystal structures of Toxoplasma gondii HGXPRTase reveal the catalytic role of a long flexible loop.,Schumacher MA, Carter D, Ross DS, Ullman B, Brennan RG Nat Struct Biol. 1996 Oct;3(10):881-7. PMID:8836106<ref>PMID:8836106</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1dbr" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Toxgo]]
[[Category: Toxoplasma gondii]]
[[Category: Brennan, R G]]
[[Category: Brennan RG]]
[[Category: Carter, D]]
[[Category: Carter D]]
[[Category: Roos, D]]
[[Category: Roos D]]
[[Category: Schumacher, M A]]
[[Category: Schumacher MA]]
[[Category: Ullman, B]]
[[Category: Ullman B]]
[[Category: Glycosyltransferase]]
[[Category: Purine salvage]]
[[Category: Transferase]]

Latest revision as of 06:51, 7 February 2024

HYPOXANTHINE GUANINE XANTHINE

1dbr, resolution 2.40Å

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