1g7o: Difference between revisions
New page: left|200px<br /><applet load="1g7o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g7o" /> '''NMR SOLUTION STRUCTURE OF REDUCED E. COLI GL... |
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== | ==NMR SOLUTION STRUCTURE OF REDUCED E. COLI GLUTAREDOXIN 2== | ||
Glutaredoxin 2 (Grx2) from Escherichia coli is distinguished from other | <StructureSection load='1g7o' size='340' side='right'caption='[[1g7o]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1g7o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G7O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G7O FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1g7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g7o OCA], [https://pdbe.org/1g7o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g7o RCSB], [https://www.ebi.ac.uk/pdbsum/1g7o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g7o ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/GLRX2_ECOLI GLRX2_ECOLI] Involved in reducing some disulfide bonds in a coupled system with glutathione reductase. Does not act as hydrogen donor for ribonucleotide 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/g7/1g7o_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=1g7o ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Glutaredoxin 2 (Grx2) from Escherichia coli is distinguished from other glutaredoxins by its larger size, low overall sequence identity and lack of electron donor activity with ribonucleotide reductase. However, catalysis of glutathione (GSH)-dependent general disulfide reduction by Grx2 is extremely efficient. The high-resolution solution structure of E. coli Grx2 shows a two-domain protein, with residues 1 to 72 forming a classical "thioredoxin-fold" glutaredoxin domain, connected by an 11 residue linker to the highly helical C-terminal domain, residues 84 to 215. The active site, Cys9-Pro10-Tyr11-Cys12, is buried in the interface between the two domains, but Cys9 is solvent-accessible, consistent with its role in catalysis. The structures reveal the hither to unknown fact that Grx2 is structurally similar to glutathione-S-transferases (GST), although there is no obvious sequence homology. The similarity of these structures gives important insights into the functional significance of a new class of mammalian GST-like proteins, the single-cysteine omega class, which have glutaredoxin oxidoreductase activity rather than GSH-S-transferase conjugating activity. E. coli Grx 2 is structurally and functionally a member of this new expanding family of large glutaredoxins. The primary function of Grx2 as a GST-like glutaredoxin is to catalyze reversible glutathionylation of proteins with GSH in cellular redox regulation including stress responses. | |||
Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione-S-transferases.,Xia B, Vlamis-Gardikas A, Holmgren A, Wright PE, Dyson HJ J Mol Biol. 2001 Jul 20;310(4):907-18. PMID:11453697<ref>PMID:11453697</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1g7o" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Dyson | [[Category: Dyson HJ]] | ||
[[Category: Holmgren | [[Category: Holmgren A]] | ||
[[Category: Vlamis-Gardikas | [[Category: Vlamis-Gardikas A]] | ||
[[Category: Wright | [[Category: Wright PE]] | ||
[[Category: Xia | [[Category: Xia B]] | ||
Latest revision as of 11:30, 22 May 2024
NMR SOLUTION STRUCTURE OF REDUCED E. COLI GLUTAREDOXIN 2NMR SOLUTION STRUCTURE OF REDUCED E. COLI GLUTAREDOXIN 2
Structural highlights
FunctionGLRX2_ECOLI Involved in reducing some disulfide bonds in a coupled system with glutathione reductase. Does not act as hydrogen donor for ribonucleotide reductase. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedGlutaredoxin 2 (Grx2) from Escherichia coli is distinguished from other glutaredoxins by its larger size, low overall sequence identity and lack of electron donor activity with ribonucleotide reductase. However, catalysis of glutathione (GSH)-dependent general disulfide reduction by Grx2 is extremely efficient. The high-resolution solution structure of E. coli Grx2 shows a two-domain protein, with residues 1 to 72 forming a classical "thioredoxin-fold" glutaredoxin domain, connected by an 11 residue linker to the highly helical C-terminal domain, residues 84 to 215. The active site, Cys9-Pro10-Tyr11-Cys12, is buried in the interface between the two domains, but Cys9 is solvent-accessible, consistent with its role in catalysis. The structures reveal the hither to unknown fact that Grx2 is structurally similar to glutathione-S-transferases (GST), although there is no obvious sequence homology. The similarity of these structures gives important insights into the functional significance of a new class of mammalian GST-like proteins, the single-cysteine omega class, which have glutaredoxin oxidoreductase activity rather than GSH-S-transferase conjugating activity. E. coli Grx 2 is structurally and functionally a member of this new expanding family of large glutaredoxins. The primary function of Grx2 as a GST-like glutaredoxin is to catalyze reversible glutathionylation of proteins with GSH in cellular redox regulation including stress responses. Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione-S-transferases.,Xia B, Vlamis-Gardikas A, Holmgren A, Wright PE, Dyson HJ J Mol Biol. 2001 Jul 20;310(4):907-18. PMID:11453697[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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