1oc3: Difference between revisions
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[[Image:1oc3.gif|left|200px]]<br /> | [[Image:1oc3.gif|left|200px]]<br /><applet load="1oc3" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1oc3" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1oc3, resolution 2.00Å" /> | caption="1oc3, resolution 2.00Å" /> | ||
'''HUMAN PEROXIREDOXIN 5'''<br /> | '''HUMAN PEROXIREDOXIN 5'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1OC3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with BEZ as [http://en.wikipedia.org/wiki/ligand ligand]. | 1OC3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with BEZ as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Bez Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OC3 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transit peptide]] | [[Category: transit peptide]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 17:23:07 2007'' | ||
Revision as of 18:13, 18 December 2007
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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 BEZ 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
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