From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1fa8.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1fa8.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1fa8| PDB=1fa8 | SCENE= }} | | {{STRUCTURE_1fa8| PDB=1fa8 | SCENE= }} |
| | | | |
| - | '''CRYSTAL STRUCTURE OF THE APO FORM GLYOXALASE I OF ESCHERICHIA COLI'''
| + | ===CRYSTAL STRUCTURE OF THE APO FORM 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. | + | 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. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_10913283}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 30: |
Line 34: |
| | [[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 16:05:38 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:56:51 2008'' |
Revision as of 23:56, 30 June 2008
Template:STRUCTURE 1fa8
CRYSTAL STRUCTURE OF THE APO FORM GLYOXALASE I OF ESCHERICHIA COLI
Template:ABSTRACT PUBMED 10913283
About this Structure
1FA8 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
Page seeded by OCA on Tue Jul 1 02:56:51 2008
