1sg3: Difference between revisions

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 <StructureSection load='1sg3' size='340' side='right'caption='[[1sg3]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1sg3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SG3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SG3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1sg3]] is a 2 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=1SG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SG3 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DAL2, ALC1, YIR029W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
+</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>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Allantoicase Allantoicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.4 3.5.3.4] </span></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=1sg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sg3 OCA], [https://pdbe.org/1sg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sg3 RCSB], [https://www.ebi.ac.uk/pdbsum/1sg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sg3 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1sg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sg3 OCA], [http://pdbe.org/1sg3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sg3 RCSB], [http://www.ebi.ac.uk/pdbsum/1sg3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sg3 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ALLC_YEAST ALLC_YEAST]] Utilization of purines as secondary nitrogen sources, when primary sources are limiting.
+[https://www.uniprot.org/uniprot/ALLC_YEAST ALLC_YEAST] Utilization of purines as secondary nitrogen sources, when primary sources are limiting.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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=1sg3 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Allantoicase (EC 3.5.3.4) catalyzes the conversion of allantoate into ureidoglycolate and urea, one of the final steps in the degradation of purines to urea. The mechanism of most enzymes involved in this pathway, which has been known for a long time, is unknown. In this paper we describe the three-dimensional crystal structure of the yeast allantoicase determined at a resolution of 2.6 A by single anomalous diffraction. This constitutes the first structure for an enzyme of this pathway. The structure reveals a repeated jelly roll beta-sheet motif, also present in proteins of unrelated biochemical function. Allantoicase has a hexameric arrangement in the crystal (dimer of trimers). Analysis of the protein sequence against the structural data reveals the presence of two totally conserved surface patches, one on each jelly roll motif. The hexameric packing concentrates these patches into conserved pockets that probably constitute the active site.
-Crystal structure of yeast allantoicase reveals a repeated jelly roll motif.,Leulliot N, Quevillon-Cheruel S, Sorel I, Graille M, Meyer P, Liger D, Blondeau K, Janin J, van Tilbeurgh H J Biol Chem. 2004 May 28;279(22):23447-52. Epub 2004 Mar 12. PMID:15020593<ref>PMID:15020593</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1sg3" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Allantoicase]]
-[[Category: Atcc 18824]]
 [[Category: Large Structures]]
-[[Category: Blondeau, K]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Graille, M]]
+[[Category: Blondeau K]]
-[[Category: Janin, J]]
+[[Category: Graille M]]
-[[Category: Leulliot, N]]
+[[Category: Janin J]]
-[[Category: Liger, D]]
+[[Category: Leulliot N]]
-[[Category: Meyer, P]]
+[[Category: Liger D]]
-[[Category: Quevillon-Cheruel, S]]
+[[Category: Meyer P]]
-[[Category: Sorel, I]]
+[[Category: Quevillon-Cheruel S]]
-[[Category: Tilbeurgh, H van]]
+[[Category: Sorel I]]
-[[Category: Hexamer]]
+[[Category: Van Tilbeurgh H]]
-[[Category: Hydrolase]]
-[[Category: Jelly roll]]