1f9z: Difference between revisions

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[[Image:1f9z.jpg|left|200px]]


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==CRYSTAL STRUCTURE OF THE NI(II)-BOUND GLYOXALASE I FROM ESCHERICHIA COLI==
The line below this paragraph, containing "STRUCTURE_1f9z", creates the "Structure Box" on the page.
<StructureSection load='1f9z' size='340' side='right'caption='[[1f9z]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1f9z]] 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=1F9Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F9Z FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
{{STRUCTURE_1f9z| PDB=1f9z |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f9z OCA], [https://pdbe.org/1f9z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f9z RCSB], [https://www.ebi.ac.uk/pdbsum/1f9z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f9z 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/f9/1f9z_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=1f9z ConSurf].
<div style="clear:both"></div>


'''CRYSTAL STRUCTURE OF THE NI(II)-BOUND GLYOXALASE I FROM ESCHERICHIA COLI'''
==See Also==
 
*[[Glyoxalase 3D structures|Glyoxalase 3D structures]]
 
== References ==
==Overview==
<references/>
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.
__TOC__
 
</StructureSection>
==About this Structure==
1F9Z 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=1F9Z OCA].
 
==Reference==
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]
[[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: Beta-alpha-beta-beta-beta motif]]
[[Category: Homodimer]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:05:14 2008''

Latest revision as of 10:12, 7 February 2024

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

Structural highlights

1f9z 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 1.5Å
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

1f9z, resolution 1.50Å

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