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=''> | ||
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<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 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 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 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 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> | <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://pdbe.org/4mjb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mjb RCSB], [http://www.ebi.ac.uk/pdbsum/4mjb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mjb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4mjb" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> |
Revision as of 10:30, 5 August 2016
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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