3grx: Difference between revisions
New page: left|200px<br /><applet load="3grx" size="450" color="white" frame="true" align="right" spinBox="true" caption="3grx" /> '''NMR STRUCTURE OF ESCHERICHIA COLI GLUTAREDOX... |
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== | ==NMR STRUCTURE OF ESCHERICHIA COLI GLUTAREDOXIN 3-GLUTATHIONE MIXED DISULFIDE COMPLEX, 20 STRUCTURES== | ||
Glutaredoxins (Grxs) catalyze reversible oxidation/reduction of protein | <StructureSection load='3grx' size='340' side='right'caption='[[3grx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | |||
<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> | |||
</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> | |||
<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> | |||
</table> | |||
== Function == | |||
[[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. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gr/3grx_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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. | |||
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 MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 3grx" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Aslund, F | <references/> | ||
[[Category: Berndt, K | __TOC__ | ||
[[Category: Holmgren, A | </StructureSection> | ||
[[Category: Nordstrand, K | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Otting, G | [[Category: Large Structures]] | ||
[[Category: | [[Category: Aslund, F]] | ||
[[Category: Berndt, K D]] | |||
[[Category: | [[Category: Holmgren, A]] | ||
[[Category: | [[Category: Nordstrand, K]] | ||
[[Category: | [[Category: Otting, G]] | ||
[[Category: Electron transport]] | |||
[[Category: Thiol-disulfide oxidoreductase]] | |||
[[Category: Thioltransferase]] | |||
[[Category: Thioredoxin superfamily]] | |||
