1J30
The crystal structure of sulerythrin, a rubrerythrin-like protein from a strictly aerobic and thermoacidiphilic archaeon
Summary for 1J30
Entry DOI | 10.2210/pdb1j30/pdb |
Descriptor | 144aa long hypothetical rubrerythrin, FE (III) ION, ZINC ION, ... (5 entities in total) |
Functional Keywords | rubrerythrin, sulerythrin, sulfolobus tokodaii strain 7, four-helix bundle, domain swapping, metal binding site plasticity, structural genomics, electron transport |
Biological source | Sulfolobus tokodaii |
Total number of polymer chains | 2 |
Total formula weight | 32502.66 |
Authors | Fushinobu, S.,Shoun, H.,Wakagi, T. (deposition date: 2003-01-16, release date: 2003-10-14, Last modification date: 2023-10-25) |
Primary citation | Fushinobu, S.,Shoun, H.,Wakagi, T. The Crystal Structure of Sulerythrin, A Rubrerythrin-like Protein from A Strictly Aerobic Archaeon, Sulfolobus tokodaii strain 7, shows unexpected domain swapping Biochemistry, 42:11707-11715, 2003 Cited by PubMed Abstract: 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. PubMed: 14529281DOI: 10.1021/bi034220b PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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