1fa7

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[[Image:1fa7.jpg|left|200px]]
[[Image:1fa7.jpg|left|200px]]
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{{Structure
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|PDB= 1fa7 |SIZE=350|CAPTION= <scene name='initialview01'>1fa7</scene>, resolution 1.9&Aring;
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The line below this paragraph, containing "STRUCTURE_1fa7", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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{{STRUCTURE_1fa7| PDB=1fa7 | SCENE= }}
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|RELATEDENTRY=[[1f9z|1F9Z]], [[1fa5|1FA5]], [[1fa6|1FA6]], [[1fa8|1FA8]], [[1fro|1fro]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fa7 OCA], [http://www.ebi.ac.uk/pdbsum/1fa7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fa7 RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF CD(II)-BOUND GLYOXALASE I OF ESCHERICHIA COLI'''
'''CRYSTAL STRUCTURE OF CD(II)-BOUND GLYOXALASE I OF ESCHERICHIA COLI'''
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[[Category: Honek, J F.]]
[[Category: Honek, J F.]]
[[Category: Matthews, B W.]]
[[Category: Matthews, B W.]]
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[[Category: beta-alpha-beta-beta-beta motif]]
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[[Category: Beta-alpha-beta-beta-beta motif]]
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[[Category: homodimer]]
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[[Category: Homodimer]]
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[[Category: protein-cd(ii) complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:05:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:18:57 2008''
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Revision as of 13:05, 2 May 2008

Template:STRUCTURE 1fa7

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 Page seeded by OCA on Fri May 2 16:05:41 2008

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