1vlp
From Proteopedia
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(New page: 200px<br /><applet load="1vlp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vlp, resolution 1.75Å" /> '''Crystal structure of...) |
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| - | [[Image:1vlp.gif|left|200px]]<br /><applet load="1vlp" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1vlp, resolution 1.75Å" /> | ||
| - | '''Crystal structure of nicotinate phosphoribosyltransferase (yor209c) from Saccharomyces cerevisiae at 1.75 A resolution'''<br /> | ||
| - | == | + | ==Crystal structure of a putative nicotinate phosphoribosyltransferase (yor209c, npt1) from saccharomyces cerevisiae at 1.75 A resolution== |
| - | + | <StructureSection load='1vlp' size='340' side='right'caption='[[1vlp]], [[Resolution|resolution]] 1.75Å' scene=''> | |
| - | [ | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[1vlp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VLP FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1vlp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vlp OCA], [https://pdbe.org/1vlp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vlp RCSB], [https://www.ebi.ac.uk/pdbsum/1vlp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vlp ProSAT], [https://www.topsan.org/Proteins/JCSG/1vlp TOPSAN]</span></td></tr> | |
| - | [ | + | </table> |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/NPT1_YEAST NPT1_YEAST] Essential for growth under anaerobic conditions.<ref>PMID:12062417</ref> Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP (By similarity).<ref>PMID:12062417</ref> | |
| - | [ | + | == Evolutionary Conservation == |
| - | [[ | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | [ | + | Check<jmol> |
| - | [[ | + | <jmolCheckbox> |
| - | [ | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vl/1vlp_consurf.spt"</scriptWhenChecked> |
| - | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |
| - | + | <text>to colour the structure by Evolutionary Conservation</text> | |
| - | + | </jmolCheckbox> | |
| + | </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=1vlp ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Nicotinamide adenine dinucleotide (NAD) is an essential cofactor for cellular redox reactions and can act as an important substrate in numerous biological processes. As a result, nature has evolved multiple biosynthetic pathways to meet this high chemical demand. In Saccharomyces cerevisiae, the NAD salvage pathway relies on the activity of nicotinic acid phosphoribosyltransferase (NAPRTase), a member of the phosphoribosyltransferase (PRTase) superfamily. Here, we report the structure of a eukaryotic (yeast) NAPRTase at 1.75 A resolution (locus name: YOR209C, gene name: NPT1). The structure reveals a two-domain fold that resembles the architecture of quinolinic acid phosphoribosyltransferases (QAPRTases), but with completely different dispositions that provide evidence for structural heterogeneity among the Type II PRTases. The identification of a third domain in NAPRTases provides a structural basis and possible mechanism for the functional modulation of this family of enzymes by ATP. | ||
| - | + | The structure of a eukaryotic nicotinic acid phosphoribosyltransferase reveals structural heterogeneity among type II PRTases.,Chappie JS, Canaves JM, Han GW, Rife CL, Xu Q, Stevens RC Structure. 2005 Sep;13(9):1385-96. PMID:16154095<ref>PMID:16154095</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 1vlp" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae]] | ||
Current revision
Crystal structure of a putative nicotinate phosphoribosyltransferase (yor209c, npt1) from saccharomyces cerevisiae at 1.75 A resolution
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