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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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9218781 (full description)]]
<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==
1FRO 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: 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 Tue Oct 30 13:18:43 2007''

Latest revision as of 07:18, 7 February 2024

HUMAN GLYOXALASE I WITH BENZYL-GLUTATHIONE INHIBITOR

1fro, resolution 2.20Å

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