1mej: Difference between revisions

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-[[Image:1mej.png|left|200px]]
-{{STRUCTURE_1mej|  PDB=1mej  |  SCENE=  }}
+==Human Glycinamide Ribonucleotide Transformylase domain at pH 8.5==
+<StructureSection load='1mej' size='340' side='right'caption='[[1mej]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1mej]] is a 3 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=1MEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MEJ 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]] 2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=1mej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mej OCA], [https://pdbe.org/1mej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mej RCSB], [https://www.ebi.ac.uk/pdbsum/1mej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mej ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PUR2_HUMAN PUR2_HUMAN]
+== 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/me/1mej_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=1mej ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Glycinamide ribonucleotide transformylase (GAR Tfase) is a key folate-dependent enzyme in the de novo purine biosynthesis pathway and, as such, has been the target for antitumor drug design. Here, we describe the crystal structures of the human GAR Tfase (purN) component of the human trifunctional protein (purD-purM-purN) at various pH values and in complex with its substrate. Human GAR Tfase exhibits pH-dependent enzyme activity with its maximum around pH 7.5-8. Comparison of unliganded human GAR Tfase structures at pH 4.2 and pH 8.5 reveals conformational differences in the substrate binding loop, which at pH 4.2 occupies the binding cleft and prohibits substrate binding, while at pH 8.5 is permissive for substrate binding. The crystal structure of GAR Tfase with its natural substrate, beta-glycinamide ribonucleotide (beta-GAR), at pH 8.5 confirms this conformational isomerism. Surprisingly, several important structural differences are found between human GAR Tfase and previously reported E. coli GAR Tfase structures, which have been used as the primary template for drug design studies. While the E. coli structure gave valuable insights into the active site and formyl transfer mechanism, differences in structure and inhibition between the bacterial and mammalian enzymes suggest that the human GAR Tfase structure is now the appropriate template for the design of anti-cancer agents.
-===Human Glycinamide Ribonucleotide Transformylase domain at pH 8.5===
+Crystal structures of human GAR Tfase at low and high pH and with substrate beta-GAR.,Zhang Y, Desharnais J, Greasley SE, Beardsley GP, Boger DL, Wilson IA Biochemistry. 2002 Dec 3;41(48):14206-15. PMID:12450384<ref>PMID:12450384</ref>
-{{ABSTRACT_PUBMED_12450384}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 1mej" style="background-color:#fffaf0;"></div>
-[[1mej]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MEJ OCA].
+== References ==
+<references/>
-==Reference==
+__TOC__
-<ref group="xtra">PMID:012450384</ref><references group="xtra"/>
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Phosphoribosylglycinamide formyltransferase]]
+[[Category: Large Structures]]
-[[Category: Beardsley, G P.]]
+[[Category: Beardsley GP]]
-[[Category: Boger, D L.]]
+[[Category: Boger DL]]
-[[Category: Desharnais, J.]]
+[[Category: Desharnais J]]
-[[Category: Greasley, S E.]]
+[[Category: Greasley SE]]
-[[Category: Wilson, I A.]]
+[[Category: Wilson IA]]
-[[Category: Zhang, Y.]]
+[[Category: Zhang Y]]
-[[Category: Purine biosynthesis]]
-[[Category: Transferase]]