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| [[Image:1f9z.jpg|left|200px]] | | {{Seed}} |
| | [[Image:1f9z.png|left|200px]] |
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| {{STRUCTURE_1f9z| PDB=1f9z | SCENE= }} | | {{STRUCTURE_1f9z| PDB=1f9z | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF THE NI(II)-BOUND GLYOXALASE I FROM ESCHERICHIA COLI'''
| | ===CRYSTAL STRUCTURE OF THE NI(II)-BOUND GLYOXALASE I FROM ESCHERICHIA COLI=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_10913283}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10913283 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10913283}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Beta-alpha-beta-beta-beta motif]] | | [[Category: Beta-alpha-beta-beta-beta motif]] |
| [[Category: Homodimer]] | | [[Category: Homodimer]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:05:14 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:56:15 2008'' |