1fov: Difference between revisions

Revision as of 13:40, 21 February 2008

GLUTAREDOXIN 3 FROM ESCHERICHIA COLI IN THE FULLY OXIDIZED FORM

OverviewOverview

A high precision NMR structure of oxidized glutaredoxin 3 [C65Y] from Escherichia coli has been determined. The conformation of the active site including the disulphide bridge is highly similar to those in glutaredoxins from pig liver and T4 phage. A comparison with the previously determined structure of glutaredoxin 3 [C14S, C65Y] in a complex with glutathione reveals conformational changes between the free and substrate-bound form which includes the sidechain of the conserved, active site tyrosine residue. In the oxidized form this tyrosine is solvent exposed, while it adopts a less exposed conformation, stabilized by hydrogen bonds, in the mixed disulfide with glutathione. The structures further suggest that the formation of a covalent linkage between glutathione and glutaredoxin 3 is necessary in order to induce these structural changes upon binding of the glutathione peptide. This could explain the observed low affinity of glutaredoxins for S-blocked glutathione analogues, in spite of the fact that glutaredoxins are highly specific reductants of glutathione mixed disulfides.

About this StructureAbout this Structure

1FOV is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

NMR structure of oxidized glutaredoxin 3 from Escherichia coli., Nordstrand K, Sandstrom A, Aslund F, Holmgren A, Otting G, Berndt KD, J Mol Biol. 2000 Oct 27;303(3):423-32. PMID:11031118

Page seeded by OCA on Thu Feb 21 12:40:57 2008

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OCA

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-[[Image:1fov.gif|left|200px]]<br /><applet load="1fov" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1fov.gif|left|200px]]<br /><applet load="1fov" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1fov" />
 '''GLUTAREDOXIN 3 FROM ESCHERICHIA COLI IN THE FULLY OXIDIZED FORM'''<br />
 ==Overview==
-A high precision NMR structure of oxidized glutaredoxin 3 [C65Y] from, Escherichia coli has been determined. The conformation of the active site, including the disulphide bridge is highly similar to those in, glutaredoxins from pig liver and T4 phage. A comparison with the, previously determined structure of glutaredoxin 3 [C14S, C65Y] in a, complex with glutathione reveals conformational changes between the free, and substrate-bound form which includes the sidechain of the conserved, active site tyrosine residue. In the oxidized form this tyrosine is, solvent exposed, while it adopts a less exposed conformation, stabilized, by hydrogen bonds, in the mixed disulfide with glutathione. The structures, further suggest that the formation of a covalent linkage between, glutathione and glutaredoxin 3 is necessary in order to induce these, structural changes upon binding of the glutathione peptide. This could, explain the observed low affinity of glutaredoxins for S-blocked, glutathione analogues, in spite of the fact that glutaredoxins are highly, specific reductants of glutathione mixed disulfides.
+A high precision NMR structure of oxidized glutaredoxin 3 [C65Y] from Escherichia coli has been determined. The conformation of the active site including the disulphide bridge is highly similar to those in glutaredoxins from pig liver and T4 phage. A comparison with the previously determined structure of glutaredoxin 3 [C14S, C65Y] in a complex with glutathione reveals conformational changes between the free and substrate-bound form which includes the sidechain of the conserved, active site tyrosine residue. In the oxidized form this tyrosine is solvent exposed, while it adopts a less exposed conformation, stabilized by hydrogen bonds, in the mixed disulfide with glutathione. The structures further suggest that the formation of a covalent linkage between glutathione and glutaredoxin 3 is necessary in order to induce these structural changes upon binding of the glutathione peptide. This could explain the observed low affinity of glutaredoxins for S-blocked glutathione analogues, in spite of the fact that glutaredoxins are highly specific reductants of glutathione mixed disulfides.
 ==About this Structure==
-FOV 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FOV OCA].
+FOV 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=1FOV OCA].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Aslund, F.]]
-[[Category: Berndt, K.D.]]
+[[Category: Berndt, K D.]]
 [[Category: Holmgren, A.]]
 [[Category: Nordstrand, K.]]
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 [[Category: cis pro 53]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:06:13 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:57 2008''