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3grx

From Proteopedia

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[[Image:3grx.gif|left|200px]]
 
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{{Structure
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==NMR STRUCTURE OF ESCHERICHIA COLI GLUTAREDOXIN 3-GLUTATHIONE MIXED DISULFIDE COMPLEX, 20 STRUCTURES==
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|PDB= 3grx |SIZE=350|CAPTION= <scene name='initialview01'>3grx</scene>
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<StructureSection load='3grx' size='340' side='right'caption='[[3grx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=GTT:GLUTATHIONE'>GTT</scene>
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<table><tr><td colspan='2'>[[3grx]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3GRX FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3grx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3grx OCA], [https://pdbe.org/3grx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3grx RCSB], [https://www.ebi.ac.uk/pdbsum/3grx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3grx ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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'''NMR STRUCTURE OF ESCHERICHIA COLI GLUTAREDOXIN 3-GLUTATHIONE MIXED DISULFIDE COMPLEX, 20 STRUCTURES'''
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[[https://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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gr/3grx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3grx ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
Glutaredoxins (Grxs) catalyze reversible oxidation/reduction of protein disulfide groups and glutathione-containing mixed disulfide groups via an active site Grx-glutathione mixed disulfide (Grx-SG) intermediate. The NMR solution structure of the Escherichia coli Grx3 mixed disulfide with glutathione (Grx3-SG) was determined using a C14S mutant which traps this intermediate in the redox reaction. The structure contains a thioredoxin fold, with a well-defined binding site for glutathione which involves two intermolecular backbone-backbone hydrogen bonds forming an antiparallel intermolecular beta-bridge between the protein and glutathione. The solution structure of E. coli Grx3-SG also suggests a binding site for a second glutathione in the reduction of the Grx3-SG intermediate, which is consistent with the specificity of reduction observed in Grxs. Molecular details of the structure in relation to the stability of the intermediate and the activity of Grx3 as a reductant of glutathione mixed disulfide groups are discussed. A comparison of glutathione binding in Grx3-SG and ligand binding in other members of the thioredoxin superfamily is presented, which illustrates the highly conserved intermolecular interactions in this protein family.
Glutaredoxins (Grxs) catalyze reversible oxidation/reduction of protein disulfide groups and glutathione-containing mixed disulfide groups via an active site Grx-glutathione mixed disulfide (Grx-SG) intermediate. The NMR solution structure of the Escherichia coli Grx3 mixed disulfide with glutathione (Grx3-SG) was determined using a C14S mutant which traps this intermediate in the redox reaction. The structure contains a thioredoxin fold, with a well-defined binding site for glutathione which involves two intermolecular backbone-backbone hydrogen bonds forming an antiparallel intermolecular beta-bridge between the protein and glutathione. The solution structure of E. coli Grx3-SG also suggests a binding site for a second glutathione in the reduction of the Grx3-SG intermediate, which is consistent with the specificity of reduction observed in Grxs. Molecular details of the structure in relation to the stability of the intermediate and the activity of Grx3 as a reductant of glutathione mixed disulfide groups are discussed. A comparison of glutathione binding in Grx3-SG and ligand binding in other members of the thioredoxin superfamily is presented, which illustrates the highly conserved intermolecular interactions in this protein family.
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==About this Structure==
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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>
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3GRX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GRX OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9973569 9973569]
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[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Aslund, F.]]
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[[Category: Berndt, K D.]]
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[[Category: Holmgren, A.]]
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[[Category: Nordstrand, K.]]
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[[Category: Otting, G.]]
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[[Category: GTT]]
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[[Category: electron transport]]
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[[Category: thiol-disulfide oxidoreductase]]
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[[Category: thioltransferase]]
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[[Category: thioredoxin superfamily]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:05:05 2008''
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3grx" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bacillus coli migula 1895]]
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[[Category: Large Structures]]
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[[Category: Aslund, F]]
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[[Category: Berndt, K D]]
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[[Category: Holmgren, A]]
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[[Category: Nordstrand, K]]
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[[Category: Otting, G]]
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[[Category: Electron transport]]
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[[Category: Thiol-disulfide oxidoreductase]]
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[[Category: Thioltransferase]]
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[[Category: Thioredoxin superfamily]]

Current revision

NMR STRUCTURE OF ESCHERICHIA COLI GLUTAREDOXIN 3-GLUTATHIONE MIXED DISULFIDE COMPLEX, 20 STRUCTURES

PDB ID 3grx

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