4mjb: Difference between revisions
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==Synechocystis sp. PCC 6803 glutaredoxin A-A79S== | ==Synechocystis sp. PCC 6803 glutaredoxin A-A79S== | ||
<StructureSection load='4mjb' size='340' side='right' caption='[[4mjb]], [[Resolution|resolution]] 2.11Å' scene=''> | <StructureSection load='4mjb' size='340' side='right'caption='[[4mjb]], [[Resolution|resolution]] 2.11Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4mjb]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4mjb]] 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=4MJB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MJB FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.111Å</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> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4mjb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mjb OCA], [https://pdbe.org/4mjb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mjb RCSB], [https://www.ebi.ac.uk/pdbsum/4mjb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mjb ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synechocystis sp. PCC 6803 substr. Kazusa]] | ||
[[Category: | [[Category: Knaff DB]] | ||
[[Category: | [[Category: Sutton RB]] | ||
Latest revision as of 19:38, 20 September 2023
Synechocystis sp. PCC 6803 glutaredoxin A-A79SSynechocystis sp. PCC 6803 glutaredoxin A-A79S
Structural highlights
FunctionGLRX2_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 PubMedGlutaredoxin 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
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