1fa6: Difference between revisions

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 <StructureSection load='1fa6' size='340' side='right'caption='[[1fa6]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1fa6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FA6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FA6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1fa6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FA6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FA6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></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]] 1.9&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f9z|1f9z]], [[1fa5|1fa5]], [[1fa7|1fa7]], [[1fa8|1fa8]], [[1fro|1fro]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lactoylglutathione_lyase Lactoylglutathione lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.5 4.4.1.5] </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=1fa6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fa6 OCA], [https://pdbe.org/1fa6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fa6 RCSB], [https://www.ebi.ac.uk/pdbsum/1fa6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fa6 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fa6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fa6 OCA], [http://pdbe.org/1fa6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fa6 RCSB], [http://www.ebi.ac.uk/pdbsum/1fa6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fa6 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/LGUL_ECOLI LGUL_ECOLI]] Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.<ref>PMID:10913283</ref>
+[https://www.uniprot.org/uniprot/LGUL_ECOLI LGUL_ECOLI] Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.<ref>PMID:10913283</ref>
 == 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=1fa6 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The metalloenzyme glyoxalase I (GlxI) converts the nonenzymatically produced hemimercaptal of cytotoxic methylglyoxal and glutathione to nontoxic S-D-lactoylglutathione. Human GlxI, for which the structure is known, is active in the presence of Zn(2+). Unexpectedly, the Escherichia coli enzyme is inactive in the presence of Zn(2+) and is maximally active with Ni(2+). To understand this difference in metal activation and also to obtain a representative of the bacterial enzymes, the structure of E. coli Ni(2+)-GlxI has been determined. Structures have also been determined for the apo enzyme as well as complexes with Co(2+), Cd(2+), and Zn(2+). It is found that each of the protein-metal complexes that is catalytically active has octahedral geometry. This includes the complexes of the E. coli enzyme with Ni(2+), Co(2+), and Cd(2+), as well as the structures reported for the human Zn(2+) enzyme. Conversely, the complex of the E. coli enzyme with Zn(2+) has trigonal bipyramidal coordination and is inactive. This mode of coordination includes four protein ligands plus a single water molecule. In contrast, the coordination in the active forms of the enzyme includes two water molecules bound to the metal ion, suggesting that this may be a key feature of the catalytic mechanism. A comparison of the human and E. coli enzymes suggests that there are differences between the active sites that might be exploited for therapeutic use.
-Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation.,He MM, Clugston SL, Honek JF, Matthews BW Biochemistry. 2000 Aug 1;39(30):8719-27. PMID:10913283<ref>PMID:10913283</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1fa6" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 37: / Line 27: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
-[[Category: Lactoylglutathione lyase]]
 [[Category: Large Structures]]
-[[Category: Clugston, S L]]
+[[Category: Clugston SL]]
-[[Category: He, M M]]
+[[Category: He MM]]
-[[Category: Honek, J F]]
+[[Category: Honek JF]]
-[[Category: Matthews, B W]]
+[[Category: Matthews BW]]
-[[Category: Beta-alpha-beta-beta-beta motif]]
-[[Category: Homodimer]]
-[[Category: Lyase]]