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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[[Image:1g7o.jpg|left|200px]]<br /><applet load="1g7o" size=" | [[Image:1g7o.jpg|left|200px]]<br /><applet load="1g7o" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''NMR SOLUTION STRUCTURE OF REDUCED E. COLI GLUTAREDOXIN 2'''<br /> | '''NMR SOLUTION STRUCTURE OF REDUCED E. COLI GLUTAREDOXIN 2'''<br /> | ||
==Overview== | ==Overview== | ||
Glutaredoxin 2 (Grx2) from Escherichia coli is distinguished from other | 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. | ||
==About this Structure== | ==About this Structure== | ||
1G7O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | 1G7O is a [http://en.wikipedia.org/wiki/Single_protein 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=1G7O OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dyson, H | [[Category: Dyson, H J.]] | ||
[[Category: Holmgren, A.]] | [[Category: Holmgren, A.]] | ||
[[Category: Vlamis-Gardikas, A.]] | [[Category: Vlamis-Gardikas, A.]] | ||
[[Category: Wright, P | [[Category: Wright, P E.]] | ||
[[Category: Xia, B.]] | [[Category: Xia, B.]] | ||
[[Category: nmr]] | [[Category: nmr]] | ||
[[Category: reduced form of glutaredoxin]] | [[Category: reduced form of glutaredoxin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:47:01 2008'' | ||
Revision as of 13:47, 21 February 2008
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NMR SOLUTION STRUCTURE OF REDUCED E. COLI GLUTAREDOXIN 2
OverviewOverview
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.
About this StructureAbout this Structure
1G7O is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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
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