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[[Image:1fro.gif|left|200px]]<br /><applet load="1fro" size="350" 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>


==Disease==
==See Also==
Known disease associated with this structure: Autism, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=138750 138750]]
*[[Glyoxalase 3D structures|Glyoxalase 3D structures]]
 
== References ==
==About this Structure==
<references/>
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 <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=GSB:'>GSB</scene> 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] Known structural/functional Sites: <scene name='pdbsite=GH1:Binding+Site+For+Gsh+Moiety+-+Substrate+Binding+Site+Is+...'>GH1</scene>, <scene name='pdbsite=GH2:Binding+Site+For+Gsh+Moiety+-+Substrate+Binding+Site+Is+...'>GH2</scene>, <scene name='pdbsite=GH3:Binding+Site+For+Gsh+Moiety+-+Substrate+Binding+Site+Is+...'>GH3</scene>, <scene name='pdbsite=GH4:Binding+Site+For+Gsh+Moiety+-+Substrate+Binding+Site+Is+...'>GH4</scene>, <scene name='pdbsite=HD2:Hydrophobic+Substrate+Binding+Pocket+At+Dimer+Interface'>HD2</scene>, <scene name='pdbsite=HD3:Hydrophobic+Substrate+Binding+Pocket+At+Dimer+Interface'>HD3</scene>, <scene name='pdbsite=HD4:Hydrophobic+Substrate+Binding+Pocket+At+Dimer+Interface'>HD4</scene>, <scene name='pdbsite=HD5:Hydrophobic+Substrate+Binding+Pocket+At+Dimer+Interface'>HD5</scene>, <scene name='pdbsite=ZN1:Zn+Binding+Site+At+Dimer+Interface'>ZN1</scene>, <scene name='pdbsite=ZN2:Zn+Binding+Site+At+Dimer+Interface'>ZN2</scene>, <scene name='pdbsite=ZN3:Zn+Binding+Site+At+Dimer+Interface'>ZN3</scene> and <scene name='pdbsite=ZN4:Zn+Binding+Site+At+Dimer+Interface'>ZN4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FRO OCA].
__TOC__
 
</StructureSection>
==Reference==
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]
[[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://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:41:59 2008''

Latest revision as of 10:18, 7 February 2024

HUMAN GLYOXALASE I WITH BENZYL-GLUTATHIONE INHIBITORHUMAN GLYOXALASE I WITH BENZYL-GLUTATHIONE INHIBITOR

Structural highlights

1fro is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ de Hemptinne V, Rondas D, Toepoel M, Vancompernolle K. Phosphorylation on Thr-106 and NO-modification of glyoxalase I suppress the TNF-induced transcriptional activity of NF-kappaB. Mol Cell Biochem. 2009 May;325(1-2):169-78. doi: 10.1007/s11010-009-0031-7. Epub , 2009 Feb 6. PMID:19199007 doi:http://dx.doi.org/10.1007/s11010-009-0031-7

1fro, resolution 2.20Å

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