1fro: Difference between revisions

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-[[Image:1fro.gif|left|200px]]<br />
-<applet load="1fro" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1fro, resolution 2.2&Aring;" />
-'''HUMAN GLYOXALASE I WITH BENZYL-GLUTATHIONE INHIBITOR'''<br />
-==Overview==
+==HUMAN GLYOXALASE I WITH BENZYL-GLUTATHIONE INHIBITOR==
-The zinc metalloenzyme glyoxalase I catalyses the glutathione-dependent, inactivation of toxic methylglyoxal. The structure of the dimeric human, enzyme in complex with S-benzyl-glutathione has been determined by, multiple isomorphous replacement (MIR) and refined at 2.2 A resolution., Each monomer consists of two domains. Despite only low sequence homology, between them, these domains are structurally equivalent and appear to have, arisen by a gene duplication. On the other hand, there is no structural, homology to the 'glutathione binding domain' found in other, glutathione-linked proteins. 3D domain swapping of the N- and C-terminal, domains has resulted in the active site being situated in the dimer, interface, with the inhibitor and essential zinc ion interacting with side, chains from both subunits. Two structurally equivalent residues from each, domain contribute to a square pyramidal coordination of the zinc ion, rarely seen in zinc enzymes. Comparison of glyoxalase I with other known, structures shows the enzyme to belong to a new structural family which, includes the Fe2+-dependent dihydroxybiphenyl dioxygenase and the, bleomycin resistance protein. This structural family appears to allow, members to form with or without domain swapping.
+<StructureSection load='1fro' size='340' side='right'caption='[[1fro]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1fro]] is a 4 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=1FRO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FRO 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]] 2.2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSB:S-BENZYL-GLUTATHIONE'>GSB</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1fro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fro OCA], [https://pdbe.org/1fro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fro RCSB], [https://www.ebi.ac.uk/pdbsum/1fro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fro ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/LGUL_HUMAN LGUL_HUMAN] Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B.<ref>PMID:19199007</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/fr/1fro_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=1fro ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-FRO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN and GSB as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Structure known Active Sites: GH1, GH2, GH3, GH4, HD2, HD3, HD4, HD5, ZN1, ZN2, ZN3 and ZN4. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FRO OCA].
+*[[Glyoxalase 3D structures|Glyoxalase 3D structures]]
+== References ==
-==Reference==
+<references/>
-Crystal structure of human glyoxalase I--evidence for gene duplication and 3D domain swapping., Cameron AD, Olin B, Ridderstrom M, Mannervik B, Jones TA, EMBO J. 1997 Jun 16;16(12):3386-95. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9218781 9218781]
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Lactoylglutathione lyase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Cameron AD]]
-[[Category: Cameron, A.D.]]
+[[Category: Jones TA]]
-[[Category: Jones, T.A.]]
-[[Category: GSB]]
-[[Category: ZN]]
-[[Category: glyoxalase i]]
-[[Category: lactoylglutathione lyase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 16:12:44 2007''