1qq2
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(New page: 200px<br /><applet load="1qq2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qq2, resolution 2.60Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 22:45, 20 November 2007
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CRYSTAL STRUCTURE OF A MAMMALIAN 2-CYS PEROXIREDOXIN, HBP23.
Overview
Heme-binding protein 23 kDa (HBP23), a rat isoform of human, proliferation-associated gene product (PAG), is a member of the, peroxiredoxin family of peroxidases, having two conserved cysteine, residues. Recent biochemical studies have shown that HBP23/PAG is an, oxidative stress-induced and proliferation-coupled multifunctional protein, that exhibits specific bindings to c-Abl protein tyrosine kinase and heme, as well as a peroxidase activity. A 2.6-A resolution crystal structure of, rat HBP23 in oxidized form revealed an unusual dimer structure in which, the active residue Cys-52 forms a disulfide bond with conserved Cys-173, from another subunit by C-terminal tail swapping. The active site is, largely hydrophobic with partially exposed Cys-173, suggesting a reduction, mechanism of oxidized HBP23 by thioredoxin. Thus, the unusual cysteine, disulfide bond is involved in peroxidation catalysis by using thioredoxin, as the source of reducing equivalents. The structure also provides a clue, to possible interaction surfaces for c-Abl and heme. Several significant, structural differences have been found from a 1-Cys peroxiredoxin, ORF6, which lacks the C-terminal conserved cysteine corresponding to Cys-173 of, HBP23.
About this Structure
1QQ2 is a Single protein structure of sequence from Rattus norvegicus with CL as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product., Hirotsu S, Abe Y, Okada K, Nagahara N, Hori H, Nishino T, Hakoshima T, Proc Natl Acad Sci U S A. 1999 Oct 26;96(22):12333-8. PMID:10535922
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