1fa6: Difference between revisions

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New page: left|200px<br /><applet load="1fa6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fa6, resolution 1.9Å" /> '''CRYSTAL STRUCTURE OF ...
 
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'''CRYSTAL STRUCTURE OF THE CO(II)-BOUND GLYOXALASE I OF ESCHERICHIA COLI'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THE CO(II)-BOUND GLYOXALASE I OF ESCHERICHIA COLI==
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.
<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 [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='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='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='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>
</table>
== Function ==
[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]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fa/1fa6_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=1fa6 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1FA6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CO as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FA6 OCA].
*[[Glyoxalase 3D structures|Glyoxalase 3D structures]]
 
== References ==
==Reference==
<references/>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10913283 10913283]
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Lactoylglutathione lyase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Clugston SL]]
[[Category: Clugston, S.L.]]
[[Category: He MM]]
[[Category: He, M.M.]]
[[Category: Honek JF]]
[[Category: Honek, J.F.]]
[[Category: Matthews BW]]
[[Category: Matthews, B.W.]]
[[Category: CO]]
[[Category: beta-alpha-beta-beta-beta motif]]
[[Category: homodimer]]
[[Category: protein-co(ii) complex]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:45:46 2007''

Latest revision as of 10:12, 7 February 2024

CRYSTAL STRUCTURE OF THE CO(II)-BOUND GLYOXALASE I OF ESCHERICHIA COLICRYSTAL STRUCTURE OF THE CO(II)-BOUND GLYOXALASE I OF ESCHERICHIA COLI

Structural highlights

1fa6 is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LGUL_ECOLI Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.[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. ↑ He MM, Clugston SL, Honek JF, Matthews BW. Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation. Biochemistry. 2000 Aug 1;39(30):8719-27. PMID:10913283

1fa6, resolution 1.90Å

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