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1fa8

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[[Image:1fa8.jpg|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF THE APO FORM GLYOXALASE I OF ESCHERICHIA COLI==
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|PDB= 1fa8 |SIZE=350|CAPTION= <scene name='initialview01'>1fa8</scene>, resolution 1.7&Aring;
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<StructureSection load='1fa8' size='340' side='right'caption='[[1fa8]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1fa8]] 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=1FA8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FA8 FirstGlance]. <br>
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|ACTIVITY= [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]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fa8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fa8 OCA], [https://pdbe.org/1fa8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fa8 RCSB], [https://www.ebi.ac.uk/pdbsum/1fa8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fa8 ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fa/1fa8_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1fa8 ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF THE APO FORM GLYOXALASE I OF ESCHERICHIA COLI'''
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==See Also==
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*[[Glyoxalase 3D structures|Glyoxalase 3D structures]]
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== References ==
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==Overview==
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<references/>
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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.
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__TOC__
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</StructureSection>
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==About this Structure==
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1FA8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FA8 OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10913283 10913283]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Lactoylglutathione lyase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Clugston SL]]
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[[Category: Clugston, S L.]]
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[[Category: He MM]]
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[[Category: He, M M.]]
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[[Category: Honek JF]]
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[[Category: Honek, J F.]]
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[[Category: Matthews BW]]
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[[Category: Matthews, B W.]]
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[[Category: apo enzyme.]]
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[[Category: beta-alpha-beta-beta-beta motif]]
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[[Category: homodimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:06:30 2008''
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Current revision

CRYSTAL STRUCTURE OF THE APO FORM GLYOXALASE I OF ESCHERICHIA COLI

PDB ID 1fa8

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