2jbm

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[[Image:2jbm.jpg|left|200px]]<br /><applet load="2jbm" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2jbm, resolution 2.00&Aring;" />
 
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'''QPRTASE STRUCTURE FROM HUMAN'''<br />
 
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==Overview==
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==QPRTASE STRUCTURE FROM HUMAN==
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Human quinolinate phosphoribosyltransferase (EC 2.4.2.19) (hQPRTase) is a, member of the type II phosphoribosyltransferase family involved in the, catabolism of quinolinic acid (QA). It catalyses the formation of, nicotinic acid mononucleotide from quinolinic acid, which involves a, phosphoribosyl transfer reaction followed by decarboxylation. hQPRTase has, been implicated in a number of neurological conditions and in order to, study it further, we have carried out structural and kinetic studies on, recombinant hQPRTase. The structure of the fully active enzyme, overexpressed in Escherichia coli was solved using multiwavelength methods, to a resolution of 2.0 A. hQPRTase has a alpha/beta barrel fold sharing a, similar overall structure with the bacterial QPRTases. The active site of, hQPRTase is located at an alpha/beta open sandwich structure that serves, as a cup for the alpha/beta barrel of the adjacent subunit with a QA, binding site consisting of three arginine residues (R102, R138 and R161), and two lysine residues (K139 and K171). Mutation of these residues, affected substrate binding or abolished the enzymatic activity. The, kinetics of the human enzyme are different to the bacterial enzymes, studied, hQPRTase is inhibited competitively and non-competitively by one, of its substrates, 5-phosphoribosylpyrophosphate (PRPP). The human enzyme, adopts a hexameric arrangement, which places the active sites in close, proximity to each other.
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<StructureSection load='2jbm' size='340' side='right'caption='[[2jbm]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2jbm]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JBM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JBM FirstGlance]. <br>
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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&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SRT:S,R+MESO-TARTARIC+ACID'>SRT</scene></td></tr>
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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=2jbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jbm OCA], [https://pdbe.org/2jbm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jbm RCSB], [https://www.ebi.ac.uk/pdbsum/2jbm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jbm ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NADC_HUMAN NADC_HUMAN] Involved in the catabolism of quinolinic acid (QA).<ref>PMID:17868694</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/jb/2jbm_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=2jbm ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Human quinolinate phosphoribosyltransferase (EC 2.4.2.19) (hQPRTase) is a member of the type II phosphoribosyltransferase family involved in the catabolism of quinolinic acid (QA). It catalyses the formation of nicotinic acid mononucleotide from quinolinic acid, which involves a phosphoribosyl transfer reaction followed by decarboxylation. hQPRTase has been implicated in a number of neurological conditions and in order to study it further, we have carried out structural and kinetic studies on recombinant hQPRTase. The structure of the fully active enzyme overexpressed in Escherichia coli was solved using multiwavelength methods to a resolution of 2.0 A. hQPRTase has a alpha/beta barrel fold sharing a similar overall structure with the bacterial QPRTases. The active site of hQPRTase is located at an alpha/beta open sandwich structure that serves as a cup for the alpha/beta barrel of the adjacent subunit with a QA binding site consisting of three arginine residues (R102, R138 and R161) and two lysine residues (K139 and K171). Mutation of these residues affected substrate binding or abolished the enzymatic activity. The kinetics of the human enzyme are different to the bacterial enzymes studied, hQPRTase is inhibited competitively and non-competitively by one of its substrates, 5-phosphoribosylpyrophosphate (PRPP). The human enzyme adopts a hexameric arrangement, which places the active sites in close proximity to each other.
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==About this Structure==
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Structural and kinetic characterization of quinolinate phosphoribosyltransferase (hQPRTase) from homo sapiens.,Liu H, Woznica K, Catton G, Crawford A, Botting N, Naismith JH J Mol Biol. 2007 Oct 26;373(3):755-63. Epub 2007 Aug 24. PMID:17868694<ref>PMID:17868694</ref>
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2JBM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SRT:'>SRT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Nicotinate-nucleotide_diphosphorylase_(carboxylating) Nicotinate-nucleotide diphosphorylase (carboxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.19 2.4.2.19] Known structural/functional Sites: <scene name='pdbsite=AC1:Srt+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Srt+Binding+Site+For+Chain+B'>AC2</scene>, <scene name='pdbsite=AC3:Srt+Binding+Site+For+Chain+C'>AC3</scene>, <scene name='pdbsite=AC4:Srt+Binding+Site+For+Chain+D'>AC4</scene>, <scene name='pdbsite=AC5:Srt+Binding+Site+For+Chain+E'>AC5</scene>, <scene name='pdbsite=AC6:Srt+Binding+Site+For+Chain+F'>AC6</scene>, <scene name='pdbsite=AC7:Srt+Binding+Site+For+Chain+G'>AC7</scene>, <scene name='pdbsite=AC8:Srt+Binding+Site+For+Chain+H'>AC8</scene>, <scene name='pdbsite=AC9:Srt+Binding+Site+For+Chain+I'>AC9</scene>, <scene name='pdbsite=BC1:Srt+Binding+Site+For+Chain+J'>BC1</scene>, <scene name='pdbsite=BC2:Srt+Binding+Site+For+Chain+K'>BC2</scene> and <scene name='pdbsite=BC3:Srt+Binding+Site+For+Chain+L'>BC3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JBM OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structural and Kinetic Characterization of Quinolinate Phosphoribosyltransferase (hQPRTase) from Homo sapiens., Liu H, Woznica K, Catton G, Crawford A, Botting N, Naismith JH, J Mol Biol. 2007 Oct 26;373(3):755-63. Epub 2007 Aug 24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17868694 17868694]
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 2jbm" style="background-color:#fffaf0;"></div>
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[[Category: Nicotinate-nucleotide diphosphorylase (carboxylating)]]
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[[Category: Single protein]]
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[[Category: Liu, H.]]
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[[Category: Naismith, J.H.]]
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[[Category: SRT]]
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[[Category: enzyme]]
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[[Category: glycosyltransferase]]
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[[Category: metabolism]]
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[[Category: nad]]
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[[Category: polymorphism]]
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[[Category: pyridine nucleotide biosynthesis]]
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[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:43:46 2008''
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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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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Liu H]]
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[[Category: Naismith JH]]

Current revision

QPRTASE STRUCTURE FROM HUMAN

PDB ID 2jbm

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