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| | <StructureSection load='2jad' size='340' side='right'caption='[[2jad]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='2jad' size='340' side='right'caption='[[2jad]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jad]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeqvi Aeqvi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JAD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JAD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jad]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JAD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JAD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.7Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PIA:[(4Z)-2-[(1S)-1-AMINOETHYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>PIA</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PIA:[(4Z)-2-[(1S)-1-AMINOETHYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>PIA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2jad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jad OCA], [https://pdbe.org/2jad PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jad RCSB], [https://www.ebi.ac.uk/pdbsum/2jad PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jad ProSAT]</span></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=2jad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jad OCA], [https://pdbe.org/2jad PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jad RCSB], [https://www.ebi.ac.uk/pdbsum/2jad PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jad ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI]] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. | + | [https://www.uniprot.org/uniprot/GLRX1_YEAST GLRX1_YEAST] Multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage.<ref>PMID:9571241</ref> <ref>PMID:11875065</ref> <ref>PMID:12684511</ref> [https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aeqvi]] | + | [[Category: Aequorea victoria]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hakansson, K O]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Winther, J R]] | + | [[Category: Hakansson KO]] |
| - | [[Category: Electron transport]] | + | [[Category: Winther JR]] |
| - | [[Category: Glutaredoxin]]
| + | |
| - | [[Category: Grx1p]]
| + | |
| - | [[Category: Redox- active center]]
| + | |
| - | [[Category: Transport]]
| + | |
| - | [[Category: Yeast]]
| + | |
| - | [[Category: Yellow fluorescent protein]]
| + | |
| Structural highlights
Function
GLRX1_YEAST Multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage.[1] [2] [3] GFP_AEQVI Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
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
Glutathionylated glutaredoxin Grx1p C30S mutant from yeast has been crystallized in space group C222(1) and a fusion protein between redox-sensitive yellow fluorescent protein (rxYFP) and Grx1p C30S has been crystallized in space group P6(4). The structure of the latter was solved by molecular replacement using the known rxYFP structure as a search model. The structure of the Grx1p moiety was built and the structure was refined against 2.7 A synchrotron data to an R(free) of 25.7%. There are no specific contacts between the two domains, indicating that the observed enhanced exchange of reduction equivalents between them arises from diffusion or from an enhanced collision rate in solution. The Grx1p structure thus obtained was subsequently used to solve the structure of the orthorhombic crystal, which could be refined against 2.0 A data to an R(free) of 24.3%. The structure of the glutathione-bound protein and the glutaredoxin domain in the fusion protein are similar. The covalent disulfide bond between the glutathione and protein is broken upon exposure to synchrotron radiation. The structure and the glutathione-binding mode are described and compared with existing crystallographic and nuclear magnetic resonance (NMR) structures of related glutaredoxins. Conserved residues are clustered on one side of the active site.
Structure of glutaredoxin Grx1p C30S mutant from yeast.,Hakansson KO, Winther JR Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):288-94. Epub 2007, Feb 21. PMID:17327665[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Luikenhuis S, Perrone G, Dawes IW, Grant CM. The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species. Mol Biol Cell. 1998 May;9(5):1081-91. PMID:9571241
- ↑ Collinson EJ, Wheeler GL, Garrido EO, Avery AM, Avery SV, Grant CM. The yeast glutaredoxins are active as glutathione peroxidases. J Biol Chem. 2002 May 10;277(19):16712-7. Epub 2002 Mar 1. PMID:11875065 doi:http://dx.doi.org/10.1074/jbc.M111686200
- ↑ Collinson EJ, Grant CM. Role of yeast glutaredoxins as glutathione S-transferases. J Biol Chem. 2003 Jun 20;278(25):22492-7. Epub 2003 Apr 8. PMID:12684511 doi:http://dx.doi.org/10.1074/jbc.M301387200
- ↑ Hakansson KO, Winther JR. Structure of glutaredoxin Grx1p C30S mutant from yeast. Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):288-94. Epub 2007, Feb 21. PMID:17327665 doi:10.1107/S0907444906051675
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