1fa7: Difference between revisions
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'''CRYSTAL STRUCTURE OF CD(II)-BOUND GLYOXALASE I OF ESCHERICHIA COLI''' | {{Structure | ||
|PDB= 1fa7 |SIZE=350|CAPTION= <scene name='initialview01'>1fa7</scene>, resolution 1.9Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CD:CADMIUM ION'>CD</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Lactoylglutathione_lyase Lactoylglutathione lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.5 4.4.1.5] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF CD(II)-BOUND GLYOXALASE I OF ESCHERICHIA COLI''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1FA7 is a [ | 1FA7 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=1FA7 OCA]. | ||
==Reference== | ==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:// | 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: Lactoylglutathione lyase]] | ||
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[[Category: protein-cd(ii) complex]] | [[Category: protein-cd(ii) complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:06:31 2008'' | ||
Revision as of 09:06, 20 March 2008
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| 1fa7, resolution 1.9Å | |||||||||||||
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| Ligands: | CD | ||||||||||||
| Activity: | Lactoylglutathione lyase, with EC number 4.4.1.5 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF CD(II)-BOUND GLYOXALASE I OF ESCHERICHIA COLI
Overview
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.
About this Structure
1FA7 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from 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:10913283
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