4mjb: Difference between revisions
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<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 [http://en.wikipedia.org/wiki/Syny3 Syny3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MJB OCA]. <br> | <table><tr><td colspan='2'>[[4mjb]] 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=4MJB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MJB FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qmx|3qmx]], [[4mja|4mja]], [[4mjc|4mjc]], [[4mje|4mje]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qmx|3qmx]], [[4mja|4mja]], [[4mjc|4mjc]], [[4mje|4mje]]</td></tr> | ||
<tr><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> | <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> | ||
<tr | <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=4mjb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mjb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mjb RCSB], [http://www.ebi.ac.uk/pdbsum/4mjb PDBsum]</span></td></tr> | ||
</table> | |||
<table> | == 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). | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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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> | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Syny3]] | [[Category: Syny3]] | ||
[[Category: Knaff, D B | [[Category: Knaff, D B]] | ||
[[Category: Sutton, R B | [[Category: Sutton, R B]] | ||
[[Category: Electron transport]] | [[Category: Electron transport]] | ||
[[Category: Oxidation/reduction]] | [[Category: Oxidation/reduction]] | ||
[[Category: Thioredoxin fold]] | [[Category: Thioredoxin fold]] | ||
Revision as of 03:17, 25 December 2014
Synechocystis sp. PCC 6803 glutaredoxin A-A79SSynechocystis sp. PCC 6803 glutaredoxin A-A79S
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 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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