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| | ==Synechocystis sp. PCC 6803 glutaredoxin A-A75I== | | ==Synechocystis sp. PCC 6803 glutaredoxin A-A75I== |
| - | <StructureSection load='4mja' size='340' side='right' caption='[[4mja]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='4mja' size='340' side='right'caption='[[4mja]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4mja]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Syny3 Syny3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MJA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MJA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4mja]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803_substr._Kazusa Synechocystis sp. PCC 6803 substr. Kazusa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MJA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MJA FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qmx|3qmx]], [[4mjb|4mjb]], [[4mjc|4mjc]], [[4mje|4mje]]</td></tr> | + | </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=4mja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mja OCA], [https://pdbe.org/4mja PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mja RCSB], [https://www.ebi.ac.uk/pdbsum/4mja PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mja ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ssr2061 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1111708 SYNY3])</td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mja OCA], [http://pdbe.org/4mja PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mja RCSB], [http://www.ebi.ac.uk/pdbsum/4mja PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mja ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GLRX2_SYNY3 GLRX2_SYNY3]] Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins (By similarity). | + | [https://www.uniprot.org/uniprot/GLRX2_SYNY3 GLRX2_SYNY3] Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Syny3]] | + | [[Category: Large Structures]] |
| - | [[Category: Knaff, D B]] | + | [[Category: Synechocystis sp. PCC 6803 substr. Kazusa]] |
| - | [[Category: Sutton, R B]] | + | [[Category: Knaff DB]] |
| - | [[Category: Electron transport]] | + | [[Category: Sutton RB]] |
| - | [[Category: Glutaredoxin]]
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| - | [[Category: Oxidation/reduction]]
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| - | [[Category: Thioredoxin fold]]
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| Structural highlights
Function
GLRX2_SYNY3 Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins (By similarity).
Publication Abstract from PubMed
Glutaredoxin from the cyanobacterium Synechocystis sp. PCC 6803 is a small protein, containing only 88 amino acids, that participates in a large number of redox reactions, serving both as an electron donor for enzyme-catalyzed reductions and as a regulator of diverse metabolic pathways. The crystal structures of glutaredoxins from several species have been solved, including the glutaredoxin A isoform from the cyanobacterium Synechocystis sp. PCC 6803. We have utilized the small size of Synechocystis glutaredoxin A and its propensity to form protein crystals that diffract to high resolution to explore a long-standing question in biochemistry; i.e., what are the effects of mutations on protein structure and function? Taking advantage of these properties, we have initiated a long-term educational project that would examine the structural and biochemical changes in glutaredoxin as a function of single-point mutational replacements. Here, we report some of the mutational effects that we have observed to date.
Utility of Synechocystis sp. PCC 6803 glutaredoxin A as a platform to study high-resolution mutagenesis of proteins.,Knaff DB, Sutton RB Front Plant Sci. 2013 Nov 15;4:461. doi: 10.3389/fpls.2013.00461. eCollection, 2013. PMID:24298277[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Knaff DB, Sutton RB. Utility of Synechocystis sp. PCC 6803 glutaredoxin A as a platform to study high-resolution mutagenesis of proteins. Front Plant Sci. 2013 Nov 15;4:461. doi: 10.3389/fpls.2013.00461. eCollection, 2013. PMID:24298277 doi:http://dx.doi.org/10.3389/fpls.2013.00461
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