4mje
From Proteopedia
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==Synechocystis sp. PCC 6803 glutaredoxin A-R27L== | ==Synechocystis sp. PCC 6803 glutaredoxin A-R27L== | ||
| - | <StructureSection load='4mje' size='340' side='right' caption='[[4mje]], [[Resolution|resolution]] 1.20Å' scene=''> | + | <StructureSection load='4mje' size='340' side='right'caption='[[4mje]], [[Resolution|resolution]] 1.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | [[4mje]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4mje]] 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=4MJE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MJE FirstGlance]. <br> |
| - | <b> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2Å</td></tr> |
| - | <b> | + | <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> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4mje FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mje OCA], [https://pdbe.org/4mje PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mje RCSB], [https://www.ebi.ac.uk/pdbsum/4mje PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mje ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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;"> | ||
== Publication Abstract from PubMed == | == 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. | 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. | ||
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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<ref>PMID:24298277</ref> | 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<ref>PMID:24298277</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| + | </div> | ||
| + | <div class="pdbe-citations 4mje" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Synechocystis sp. PCC 6803 substr. Kazusa]] |
| - | + | [[Category: Knaff DB]] | |
| - | [[Category: | + | [[Category: Sutton RB]] |
| - | [[Category: | + | |
| - | + | ||
Current revision
Synechocystis sp. PCC 6803 glutaredoxin A-R27L
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