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| - | [[Image:2qed.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2qed| PDB=2qed | SCENE= }} | | {{STRUCTURE_2qed| PDB=2qed | SCENE= }} |
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| - | '''Crystal structure of Salmonella thyphimurium LT2 glyoxalase II'''
| + | ===Crystal structure of Salmonella thyphimurium LT2 glyoxalase II=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17764159}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17764159 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17764159}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Metallo-b-lactamase superfamily]] | | [[Category: Metallo-b-lactamase superfamily]] |
| | [[Category: Salmonella typhimurium lt2]] | | [[Category: Salmonella typhimurium lt2]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:48:56 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:18:49 2008'' |
Revision as of 20:18, 28 July 2008
Template:STRUCTURE 2qed
Crystal structure of Salmonella thyphimurium LT2 glyoxalase II
Template:ABSTRACT PUBMED 17764159
About this Structure
2QED is a Single protein structure of sequence from Salmonella typhimurium. This structure supersedes the now removed PDB entry 2obw. 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
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