1j30
From Proteopedia
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The crystal structure of sulerythrin, a rubrerythrin-like protein from a strictly aerobic and thermoacidiphilic archaeon
Overview
Sulerythrin is the first rubrerythrin-like protein to be isolated from an, aerobic organism, Sulfolobus tokodaii strain 7, and it lacks a C-terminal, rubredoxin-like FeS(4) domain. The protein purified from Sulfolobus cells, was crystallized, and the crystal structure was determined at 1.7 A, resolution. The dimer of sulerythrin exhibited "domain-swapping" at the, loop connecting alphaB and alphaC, hybrid four-helix bundles consisting of, alphaA/B and alphaC/D being formed. The structure and atomic identity of, the binuclear metal center were determined by means of anomalous, scattering analysis. The site contained 1.0 mol of hexacoordinate Fe, 0.80-0.87 mol of tetracoordinate Zn, and 0.73-0.88 mol of putative O(2), per monomer. The metal ions were found at exchanged positions compared to, those in the Fe/Zn-containing rubrerythrin from Desulfovibrio vulgaris., The results demonstrate that the binuclear metal center of, rubrerythrin-like proteins is plastic in its ability to bind metal ions.
About this Structure
1J30 is a Single protein structure of sequence from Sulfolobus tokodaii with FE, ZN and OXY as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of sulerythrin, a rubrerythrin-like protein from a strictly aerobic archaeon, Sulfolobus tokodaii strain 7, shows unexpected domain swapping., Fushinobu S, Shoun H, Wakagi T, Biochemistry. 2003 Oct 14;42(40):11707-15. PMID:14529281
Page seeded by OCA on Sat Nov 24 23:00:34 2007
