1oc3: Difference between revisions

Revision as of 15:15, 21 February 2008

HUMAN PEROXIREDOXIN 5

OverviewOverview

Peroxiredoxin 5 is the last discovered mammalian member of an ubiquitous family of peroxidases widely distributed among prokaryotes and eukaryotes. Mammalian peroxiredoxin 5 has been recently classified as an atypical 2-Cys peroxiredoxin due to the presence of a conserved peroxidatic N-terminal cysteine (Cys47) and an unconserved resolving C-terminal cysteine residue (Cys151) forming an intramolecular disulfide intermediate in the oxidized enzyme. We have recently reported the crystal structure of human peroxiredoxin 5 in its reduced form. Here, a new crystal form of human peroxiredoxin 5 is described at 2.0 A resolution. The asymmetric unit contains three polypeptide chains. Surprisingly, beside two reduced chains, the third one is oxidized although the enzyme was crystallized under initial reducing conditions in the presence of 1 mM 1,4-dithio-dl-threitol. The oxidized polypeptide chain forms an homodimer with a symmetry-related one through intermolecular disulfide bonds between Cys47 and Cys151. The formation of these disulfide bonds is accompanied by the partial unwinding of the N-terminal parts of the alpha2 helix, which, in the reduced form, contains the peroxidatic Cys47 and the alpha6 helix, which is sequentially close to the resolving residue Cys151. In each monomer of the oxidized chain, the C-terminal part including the alpha6 helix is completely reorganized and is isolated from the rest of the protein on an extended arm. In the oxidized dimer, the arm belonging to the first monomer now appears at the surface of the second subunit and vice versa.

About this StructureAbout this Structure

1OC3 is a Single protein structure of sequence from Homo sapiens with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of a dimeric oxidized form of human peroxiredoxin 5., Evrard C, Capron A, Marchand C, Clippe A, Wattiez R, Soumillion P, Knoops B, Declercq JP, J Mol Biol. 2004 Apr 9;337(5):1079-90. PMID:15046979

Page seeded by OCA on Thu Feb 21 14:15:55 2008

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OCA

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 ==Overview==
-Peroxiredoxin 5 is the last discovered mammalian member of an ubiquitous, family of peroxidases widely distributed among prokaryotes and eukaryotes., Mammalian peroxiredoxin 5 has been recently classified as an atypical, 2-Cys peroxiredoxin due to the presence of a conserved peroxidatic, N-terminal cysteine (Cys47) and an unconserved resolving C-terminal, cysteine residue (Cys151) forming an intramolecular disulfide intermediate, in the oxidized enzyme. We have recently reported the crystal structure of, human peroxiredoxin 5 in its reduced form. Here, a new crystal form of, human peroxiredoxin 5 is described at 2.0 A resolution. The asymmetric, unit contains three polypeptide chains. Surprisingly, beside two reduced, chains, the third one is oxidized although the enzyme was crystallized, under initial reducing conditions in the presence of 1 mM, 1,4-dithio-dl-threitol. The oxidized polypeptide chain forms an homodimer, with a symmetry-related one through intermolecular disulfide bonds between, Cys47 and Cys151. The formation of these disulfide bonds is accompanied by, the partial unwinding of the N-terminal parts of the alpha2 helix, which, in the reduced form, contains the peroxidatic Cys47 and the alpha6 helix, which is sequentially close to the resolving residue Cys151. In each, monomer of the oxidized chain, the C-terminal part including the alpha6, helix is completely reorganized and is isolated from the rest of the, protein on an extended arm. In the oxidized dimer, the arm belonging to, the first monomer now appears at the surface of the second subunit and, vice versa.
+Peroxiredoxin 5 is the last discovered mammalian member of an ubiquitous family of peroxidases widely distributed among prokaryotes and eukaryotes. Mammalian peroxiredoxin 5 has been recently classified as an atypical 2-Cys peroxiredoxin due to the presence of a conserved peroxidatic N-terminal cysteine (Cys47) and an unconserved resolving C-terminal cysteine residue (Cys151) forming an intramolecular disulfide intermediate in the oxidized enzyme. We have recently reported the crystal structure of human peroxiredoxin 5 in its reduced form. Here, a new crystal form of human peroxiredoxin 5 is described at 2.0 A resolution. The asymmetric unit contains three polypeptide chains. Surprisingly, beside two reduced chains, the third one is oxidized although the enzyme was crystallized under initial reducing conditions in the presence of 1 mM 1,4-dithio-dl-threitol. The oxidized polypeptide chain forms an homodimer with a symmetry-related one through intermolecular disulfide bonds between Cys47 and Cys151. The formation of these disulfide bonds is accompanied by the partial unwinding of the N-terminal parts of the alpha2 helix, which, in the reduced form, contains the peroxidatic Cys47 and the alpha6 helix, which is sequentially close to the resolving residue Cys151. In each monomer of the oxidized chain, the C-terminal part including the alpha6 helix is completely reorganized and is isolated from the rest of the protein on an extended arm. In the oxidized dimer, the arm belonging to the first monomer now appears at the surface of the second subunit and vice versa.
 ==About this Structure==
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 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Declercq, J.P.]]
+[[Category: Declercq, J P.]]
 [[Category: Evrard, C.]]
 [[Category: BEZ]]
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 [[Category: transit peptide]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:56:01 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:15:55 2008''