1x6m
From Proteopedia
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'''Crystal structure of the glutathione-dependent formaldehyde-activating enzyme (Gfa)''' | '''Crystal structure of the glutathione-dependent formaldehyde-activating enzyme (Gfa)''' | ||
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[[Category: Vorholt, J A.]] | [[Category: Vorholt, J A.]] | ||
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Revision as of 11:38, 3 May 2008
Crystal structure of the glutathione-dependent formaldehyde-activating enzyme (Gfa)
Overview
The crystal structures of glutathione-dependent formaldehyde-activating enzyme (Gfa) from Paracoccus denitrificans, which catalyzes the formation of S-hydroxymethylglutathione from formaldehyde and glutathione, and its complex with glutathione (Gfa-GTT) have been determined. Gfa has a new fold with two zinc-sulfur centers, one that is structural (zinc tetracoordinated) and one catalytic (zinc apparently tricoordinated). In Gfa-GTT, the catalytic zinc is displaced due to disulfide bond formation of glutathione with one of the zinc-coordinating cysteines. Soaking crystals of Gfa-GTT with formaldehyde restores the holoenzyme. Accordingly, the displaced zinc forms a complex by scavenging formaldehyde and glutathione. The activation of formaldehyde and of glutathione in this zinc complex favors the final nucleophilic addition, followed by relocation of zinc in the catalytic site. Therefore, the structures of Gfa and Gfa-GTT draw the critical association between a dynamic zinc redox switch and a nucleophilic addition as a new facet of the redox activity of zinc-sulfur sites.
About this Structure
1X6M is a Single protein structure of sequence from Paracoccus denitrificans. Full crystallographic information is available from OCA.
Reference
A dynamic zinc redox switch., Neculai AM, Neculai D, Griesinger C, Vorholt JA, Becker S, J Biol Chem. 2005 Jan 28;280(4):2826-30. Epub 2004 Nov 17. PMID:15548539 Page seeded by OCA on Sat May 3 14:38:20 2008
