3grx
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3grx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GRX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GRX FirstGlance]. <br> | <table><tr><td colspan='2'>[[3grx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GRX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GRX FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3grx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3grx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3grx RCSB], [http://www.ebi.ac.uk/pdbsum/3grx 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=3grx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3grx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3grx RCSB], [http://www.ebi.ac.uk/pdbsum/3grx PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/GLRX3_ECOLI GLRX3_ECOLI]] The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfide bonds in a coupled system with glutathione reductase. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism.,Nordstrand K, slund F, Holmgren A, Otting G, Berndt KD J Mol Biol. 1999 Feb 19;286(2):541-52. PMID:9973569<ref>PMID:9973569</ref> | NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism.,Nordstrand K, slund F, Holmgren A, Otting G, Berndt KD J Mol Biol. 1999 Feb 19;286(2):541-52. PMID:9973569<ref>PMID:9973569</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: Bacillus coli migula 1895]] | [[Category: Bacillus coli migula 1895]] | ||
| - | [[Category: Aslund, F | + | [[Category: Aslund, F]] |
| - | [[Category: Berndt, K D | + | [[Category: Berndt, K D]] |
| - | [[Category: Holmgren, A | + | [[Category: Holmgren, A]] |
| - | [[Category: Nordstrand, K | + | [[Category: Nordstrand, K]] |
| - | [[Category: Otting, G | + | [[Category: Otting, G]] |
[[Category: Electron transport]] | [[Category: Electron transport]] | ||
[[Category: Thiol-disulfide oxidoreductase]] | [[Category: Thiol-disulfide oxidoreductase]] | ||
[[Category: Thioltransferase]] | [[Category: Thioltransferase]] | ||
[[Category: Thioredoxin superfamily]] | [[Category: Thioredoxin superfamily]] | ||
Revision as of 10:14, 25 December 2014
NMR STRUCTURE OF ESCHERICHIA COLI GLUTAREDOXIN 3-GLUTATHIONE MIXED DISULFIDE COMPLEX, 20 STRUCTURES
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