1dbr
From Proteopedia
(Difference between revisions)
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<StructureSection load='1dbr' size='340' side='right'caption='[[1dbr]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='1dbr' size='340' side='right'caption='[[1dbr]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1dbr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <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]] 2.4Å</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> | |
== 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> | ||
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| - | From MEDLINE®/PubMed®, 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: | + | [[Category: Toxoplasma gondii]] |
| - | [[Category: Brennan | + | [[Category: Brennan RG]] |
| - | [[Category: Carter | + | [[Category: Carter D]] |
| - | [[Category: Roos | + | [[Category: Roos D]] |
| - | [[Category: Schumacher | + | [[Category: Schumacher MA]] |
| - | [[Category: Ullman | + | [[Category: Ullman B]] |
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Current revision
HYPOXANTHINE GUANINE XANTHINE
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