1fa6

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 "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Related: 1f9z, 1fa5, 1fa7, 1fa8, 1fro Activity: Lactoylglutathione lyase, with EC number 4.4.1.5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [LGUL_ECOLI] Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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:10913283 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glyoxalase

spinqualitylabelsall models 1fa6, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image