1x6m
From Proteopedia
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|PDB= 1x6m |SIZE=350|CAPTION= <scene name='initialview01'>1x6m</scene>, resolution 2.35Å | |PDB= 1x6m |SIZE=350|CAPTION= <scene name='initialview01'>1x6m</scene>, resolution 2.35Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= gfa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266 Paracoccus denitrificans]) | |GENE= gfa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266 Paracoccus denitrificans]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1xa8|1XA8]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1x6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x6m OCA], [http://www.ebi.ac.uk/pdbsum/1x6m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1x6m RCSB]</span> | ||
}} | }} | ||
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[[Category: Neculai, D.]] | [[Category: Neculai, D.]] | ||
[[Category: Vorholt, J A.]] | [[Category: Vorholt, J A.]] | ||
- | [[Category: GOL]] | ||
- | [[Category: SO4]] | ||
- | [[Category: ZN]] | ||
[[Category: 3_10 helix]] | [[Category: 3_10 helix]] | ||
[[Category: formaldehyde]] | [[Category: formaldehyde]] | ||
[[Category: zn-enzyme]] | [[Category: zn-enzyme]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:45:27 2008'' |
Revision as of 21:45, 30 March 2008
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, resolution 2.35Å | |||||||
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Ligands: | , , | ||||||
Gene: | gfa (Paracoccus denitrificans) | ||||||
Related: | 1XA8
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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
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