2qed
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Glyoxalase II is a hydrolytic enzyme part of the glyoxalase system, responsible for detoxifying several cytotoxic compounds employing | + | Glyoxalase II is a hydrolytic enzyme part of the glyoxalase system, responsible for detoxifying several cytotoxic compounds employing glutathione. Glyoxalase II belongs to the superfamily of metallo-beta-lactamases, with a conserved motif able to bind up to two metal ions in their active sites, generally zinc. Instead, several eukaryotic glyoxalases II have been characterized with different ratios of iron, zinc, and manganese ions. We have expressed a gene coding for a putative member of this enzyme superfamily from Salmonella typhimurium that we demonstrate, on the basis of its activity, to be a glyoxalase II, named GloB. Recombinant GloB expressed in Escherichia coli was purified with variable amounts of iron, zinc, and manganese. All forms display similar activities, as can be shown from protein expression in minimal medium supplemented with specific metal ions. The crystal structure of GloB solved at 1.4 A shows a protein fold and active site similar to those of its eukaryotic homologues. NMR and EPR experiments also reveal a conserved electronic structure at the metal site. GloB is therefore able to accommodate these different metal ions and to carry out the hydrolytic reaction with similar efficiencies in all cases. The metal promiscuity of this enzyme (in contrast to other members of the same superfamily) can be accounted for by the presence of a conserved Asp residue acting as a second-shell ligand that is expected to increase the hardness of the metal binding site, therefore favoring iron uptake in glyoxalases II. |
==About this Structure== | ==About this Structure== | ||
| - | 2QED is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=FE:'>FE</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure | + | 2QED is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=FE:'>FE</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 2OBW. Active as [http://en.wikipedia.org/wiki/Hydroxyacylglutathione_hydrolase Hydroxyacylglutathione hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.6 3.1.2.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QED OCA]. |
==Reference== | ==Reference== | ||
| - | Biochemical and | + | Biochemical and structural characterization of Salmonella typhimurium glyoxalase II: new insights into metal ion selectivity., Campos-Bermudez VA, Leite NR, Krog R, Costa-Filho AJ, Soncini FC, Oliva G, Vila AJ, Biochemistry. 2007 Oct 2;46(39):11069-79. Epub 2007 Sep 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17764159 17764159] |
[[Category: Hydroxyacylglutathione hydrolase]] | [[Category: Hydroxyacylglutathione hydrolase]] | ||
[[Category: Salmonella typhimurium]] | [[Category: Salmonella typhimurium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bermudez, V | + | [[Category: Bermudez, V A.Campos.]] |
[[Category: Krogh, R.]] | [[Category: Krogh, R.]] | ||
| - | [[Category: Leite, N | + | [[Category: Leite, N R.]] |
[[Category: Oliva, G.]] | [[Category: Oliva, G.]] | ||
| - | [[Category: Soncini, F | + | [[Category: Soncini, F C.]] |
| - | [[Category: Vila, A | + | [[Category: Vila, A J.]] |
[[Category: EDO]] | [[Category: EDO]] | ||
[[Category: FE]] | [[Category: FE]] | ||
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[[Category: salmonella typhimurium lt2]] | [[Category: salmonella typhimurium lt2]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:38:36 2008'' |
Revision as of 16:38, 21 February 2008
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Crystal structure of Salmonella thyphimurium LT2 glyoxalase II
Overview
Glyoxalase II is a hydrolytic enzyme part of the glyoxalase system, responsible for detoxifying several cytotoxic compounds employing glutathione. Glyoxalase II belongs to the superfamily of metallo-beta-lactamases, with a conserved motif able to bind up to two metal ions in their active sites, generally zinc. Instead, several eukaryotic glyoxalases II have been characterized with different ratios of iron, zinc, and manganese ions. We have expressed a gene coding for a putative member of this enzyme superfamily from Salmonella typhimurium that we demonstrate, on the basis of its activity, to be a glyoxalase II, named GloB. Recombinant GloB expressed in Escherichia coli was purified with variable amounts of iron, zinc, and manganese. All forms display similar activities, as can be shown from protein expression in minimal medium supplemented with specific metal ions. The crystal structure of GloB solved at 1.4 A shows a protein fold and active site similar to those of its eukaryotic homologues. NMR and EPR experiments also reveal a conserved electronic structure at the metal site. GloB is therefore able to accommodate these different metal ions and to carry out the hydrolytic reaction with similar efficiencies in all cases. The metal promiscuity of this enzyme (in contrast to other members of the same superfamily) can be accounted for by the presence of a conserved Asp residue acting as a second-shell ligand that is expected to increase the hardness of the metal binding site, therefore favoring iron uptake in glyoxalases II.
About this Structure
2QED is a Single protein structure of sequence from Salmonella typhimurium with and as ligands. This structure supersedes the now removed PDB entry 2OBW. Active as Hydroxyacylglutathione hydrolase, with EC number 3.1.2.6 Full crystallographic information is available from OCA.
Reference
Biochemical and structural characterization of Salmonella typhimurium glyoxalase II: new insights into metal ion selectivity., Campos-Bermudez VA, Leite NR, Krog R, Costa-Filho AJ, Soncini FC, Oliva G, Vila AJ, Biochemistry. 2007 Oct 2;46(39):11069-79. Epub 2007 Sep 1. PMID:17764159
Page seeded by OCA on Thu Feb 21 18:38:36 2008
Categories: Hydroxyacylglutathione hydrolase | Salmonella typhimurium | Single protein | Bermudez, V A.Campos. | Krogh, R. | Leite, N R. | Oliva, G. | Soncini, F C. | Vila, A J. | EDO | FE | Glyoxalase ii (hydroxyacylglutathione hydrolase) | Metallo-b-lactamase superfamily | Salmonella typhimurium lt2
