View source for 2jbh


==Human phosphoribosyl transferase domain containing 1==
<StructureSection load='2jbh' size='340' side='right'caption='[[2jbh]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2jbh]] is a 2 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=2JBH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JBH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5GP:GUANOSINE-5-MONOPHOSPHATE'>5GP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</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=2jbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jbh OCA], [https://pdbe.org/2jbh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jbh RCSB], [https://www.ebi.ac.uk/pdbsum/2jbh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jbh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PRDC1_HUMAN PRDC1_HUMAN] Has low, barely detectable phosphoribosyltransferase activity (in vitro). Binds GMP, IMP and alpha-D-5-phosphoribosyl 1-pyrophosphate (PRPP). Is not expected to contribute to purine metabolism or GMP salvage.
== 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/jb/2jbh_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2jbh ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human hypoxanthine-guanine phosphoribosyltransferase (HPRT) (EC 2.4.2.8) catalyzes the conversion of hypoxanthine and guanine to their respective nucleoside monophosphates. Human HPRT deficiency as a result of genetic mutations is linked to both Lesch-Nyhan disease and gout. In the present study, we have characterized phosphoribosyltransferase domain containing protein 1 (PRTFDC1), a human HPRT homolog of unknown function. The PRTFDC1 structure has been determined at 1.7 A resolution with bound GMP. The overall structure and GMP binding mode are very similar to that observed for HPRT. Using a thermal-melt assay, a nucleotide metabolome library was screened against PRTFDC1 and revealed that hypoxanthine and guanine specifically interacted with the enzyme. It was subsequently confirmed that PRTFDC1 could convert these two bases into their corresponding nucleoside monophosphate. However, the catalytic efficiency (k(cat)/K(m)) of PRTFDC1 towards hypoxanthine and guanine was only 0.26% and 0.09%, respectively, of that of HPRT. This low activity could be explained by the fact that PRTFDC1 has a Gly in the position of the proposed catalytic Asp of HPRT. In PRTFDC1, a water molecule at the position of the aspartic acid side chain position in HPRT might be responsible for the low activity observed by acting as a weak base. The data obtained in the present study indicate that PRTFDC1 does not have a direct catalytic role in the nucleotide salvage pathway.

Structural and functional studies of the human phosphoribosyltransferase domain containing protein 1.,Welin M, Egeblad L, Johansson A, Stenmark P, Wang L, Flodin S, Nyman T, Tresaugues L, Kotenyova T, Johansson I, Eriksson S, Eklund H, Nordlund P FEBS J. 2010 Dec;277(23):4920-30. doi: 10.1111/j.1742-4658.2010.07897.x., Epub 2010 Nov 5. PMID:21054786<ref>PMID:21054786</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2jbh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Arrowsmith C]]
[[Category: Berglund H]]
[[Category: Busam R]]
[[Category: Collins R]]
[[Category: Edwards A]]
[[Category: Eklund H]]
[[Category: Ericsson UB]]
[[Category: Flodin S]]
[[Category: Flores A]]
[[Category: Graslund S]]
[[Category: Hallberg BM]]
[[Category: Hammarstrom M]]
[[Category: Hogbom M]]
[[Category: Holmberg Schiavone L]]
[[Category: Johansson I]]
[[Category: Karlberg T]]
[[Category: Kotenyova T]]
[[Category: Moche M]]
[[Category: Nilsson ME]]
[[Category: Nordlund P]]
[[Category: Nyman T]]
[[Category: Ogg D]]
[[Category: Persson C]]
[[Category: Sagemark J]]
[[Category: Stenmark P]]
[[Category: Sundstrom M]]
[[Category: Thorsell AG]]
[[Category: Uppenberg J]]
[[Category: Van Den Berg S]]
[[Category: Weigelt J]]
[[Category: Welin M]]