|
|
| Line 3: |
Line 3: |
| | <StructureSection load='1xa8' size='340' side='right'caption='[[1xa8]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='1xa8' size='340' side='right'caption='[[1xa8]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1xa8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_17741 Atcc 17741]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XA8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1XA8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1xa8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XA8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XA8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1x6m|1x6m]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gfa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266 ATCC 17741])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xa8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xa8 OCA], [https://pdbe.org/1xa8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xa8 RCSB], [https://www.ebi.ac.uk/pdbsum/1xa8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xa8 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1xa8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xa8 OCA], [http://pdbe.org/1xa8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xa8 RCSB], [http://www.ebi.ac.uk/pdbsum/1xa8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xa8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GFA_PARDE GFA_PARDE]] Catalyzes the condensation of formaldehyde and glutathione to S-hydroxymethylglutathione.<ref>PMID:11741920</ref> | + | [https://www.uniprot.org/uniprot/GFA_PARDE GFA_PARDE] Catalyzes the condensation of formaldehyde and glutathione to S-hydroxymethylglutathione.<ref>PMID:11741920</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 34: |
Line 33: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 17741]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Becker, S]] | + | [[Category: Paracoccus denitrificans]] |
| - | [[Category: Griesinger, C]] | + | [[Category: Becker S]] |
| - | [[Category: Neculai, A M]] | + | [[Category: Griesinger C]] |
| - | [[Category: Neculai, D]] | + | [[Category: Neculai AM]] |
| - | [[Category: Vorholt, J A]] | + | [[Category: Neculai D]] |
| - | [[Category: Formaldehyde]]
| + | [[Category: Vorholt JA]] |
| - | [[Category: Glutathione]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: S-s bond]]
| + | |
| Structural highlights
Function
GFA_PARDE Catalyzes the condensation of formaldehyde and glutathione to S-hydroxymethylglutathione.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Goenrich M, Bartoschek S, Hagemeier CH, Griesinger C, Vorholt JA. A glutathione-dependent formaldehyde-activating enzyme (Gfa) from Paracoccus denitrificans detected and purified via two-dimensional proton exchange NMR spectroscopy. J Biol Chem. 2002 Feb 1;277(5):3069-72. Epub 2001 Dec 10. PMID:11741920 doi:10.1074/jbc.C100579200
- ↑ Neculai AM, Neculai D, Griesinger C, Vorholt JA, Becker S. A dynamic zinc redox switch. J Biol Chem. 2005 Jan 28;280(4):2826-30. Epub 2004 Nov 17. PMID:15548539 doi:10.1074/jbc.C400517200
|
