1g7o

<StructureSection load='1g7o' size='340' side='right'caption='[[1g7o]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1g7o]] 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=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='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>

[[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.

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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Bacillus coli migula 1895]]

[[Category: Dyson, H J]]

[[Category: Holmgren, A]]

[[Category: Vlamis-Gardikas, A]]

[[Category: Wright, P E]]

[[Category: Xia, B]]

[[Category: Reduced form of glutaredoxin]]