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1sto

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[[Image:1sto.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF OROTATE PHOSPHORIBOSYLTRANSFERASE==
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|PDB= 1sto |SIZE=350|CAPTION= <scene name='initialview01'>1sto</scene>, resolution 2.6&Aring;
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<StructureSection load='1sto' size='340' side='right'caption='[[1sto]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene> and <scene name='pdbligand=OMP:OROTIDINE-5'-MONOPHOSPHATE'>OMP</scene>
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<table><tr><td colspan='2'>[[1sto]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1STO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1STO FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Orotate_phosphoribosyltransferase Orotate phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.10 2.4.2.10]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=OMP:OROTIDINE-5-MONOPHOSPHATE'>OMP</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sto FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sto OCA], [https://pdbe.org/1sto PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sto RCSB], [https://www.ebi.ac.uk/pdbsum/1sto PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sto ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PYRE_SALTY PYRE_SALTY] Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP) (By similarity).<ref>PMID:2271660</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/st/1sto_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1sto ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF OROTATE PHOSPHORIBOSYLTRANSFERASE'''
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==See Also==
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*[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]]
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== References ==
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==Overview==
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<references/>
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Phosphoribosyltransferases (PRTases) are enzymes involved in the synthesis of purine, pyrimidine, and pyridine nucleotides. They utilize alpha-D-5-phosphoribosyl-1-pyrophosphate (PRPP) and a nitrogenous base to form a beta-N-riboside monophosphate and pyrophosphate (PPi), and their functional significance in nucleotide homeostasis is evidenced by the devastating effects of inherited diseases associated with the decreased activity and/or stability of these enzymes. The 2.6-A structure of the Salmonella typhimurium orotate phosphoribosyltransferase (OPRTase) complexed with its product orotidine monophosphate (OMP) provides the first detailed image of a member of this group of enzymes. The OPRTase three-dimensional structure was solved using multiple isomorphous replacement methods and reveals two major features: a core five-stranded alpha/beta twisted sheet and an N-terminal region that partially covers the C-terminal portion of the core. PRTases show a very high degree of base specificity. In OPRTase, this is determined by steric constraints and the position of hydrogen bond donors/acceptors of a solvent-inaccessible crevice where the orotate ring of bound OMP resides. Crystalline OPRTase is a dimer, with catalytically important residues from each subunit available to the neighboring subunit, suggesting that oligomerization is necessary for its activity. On the basis of the presence of a common PRPP binding motif among PRTases and the similar chemistry these enzymes perform, we propose that the alpha/beta core found in OPRTase will represent a common feature for PRTases. This generality is demonstrated by construction of a model of the human hypoxanthine-guanine phosphoribosyltransferase (HGPRTase) from secondary structure predictions for HGPRTase and the three-dimensional structure of OPRTase.
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1STO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1STO OCA].
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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[[Category: Grubmeyer C]]
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==Reference==
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[[Category: Sacchettini JC]]
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Crystal structure of orotate phosphoribosyltransferase., Scapin G, Grubmeyer C, Sacchettini JC, Biochemistry. 1994 Feb 15;33(6):1287-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8312245 8312245]
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[[Category: Scapin G]]
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[[Category: Orotate phosphoribosyltransferase]]
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[[Category: Salmonella typhimurium]]
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[[Category: Single protein]]
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[[Category: Grubmeyer, C.]]
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[[Category: Sacchettini, J C.]]
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[[Category: Scapin, G.]]
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[[Category: OH]]
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[[Category: OMP]]
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[[Category: phosphoribosyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:09:31 2008''
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Current revision

CRYSTAL STRUCTURE OF OROTATE PHOSPHORIBOSYLTRANSFERASE

PDB ID 1sto

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