1HRS
A CRYSTALLOGRAPHIC STUDY OF HAEM BINDING TO FERRITIN
Summary for 1HRS
| Entry DOI | 10.2210/pdb1hrs/pdb |
| Descriptor | APOFERRITIN CO-CRYSTALLIZED WITH SN-PROTOPORPHYRIN IX IN CADMIUM SULFATE, CADMIUM ION, PROTOPORPHYRIN IX, ... (4 entities in total) |
| Functional Keywords | iron storage |
| Biological source | Equus caballus (horse) |
| Total number of polymer chains | 1 |
| Total formula weight | 20659.91 |
| Authors | Precigoux, G.,Yariv, J.,Gallois, B.,Dautant, A.,Courseille, C.,Langlois D'Estaintot, B. (deposition date: 1993-11-05, release date: 1994-05-31, Last modification date: 2024-02-07) |
| Primary citation | Precigoux, G.,Yariv, J.,Gallois, B.,Dautant, A.,Courseille, C.,d'Estaintot, B.L. A crystallographic study of haem binding to ferritin. Acta Crystallogr.,Sect.D, 50:739-743, 1994 Cited by PubMed Abstract: Ferritin, the iron-storage protein, binds porphyrins, metalloporphyrins and the fluorescent dyes ANS (8-anilino-1-naphthalenesulfonic acid) and TNS (2-p-toluidinyl-6-naphthalenesulfonic acid), similarly to apo-myoglobin. Octahedral crystals of horse-spleen apo-ferritin (HSF; 174 amino acids) complexes prepared by the addition of haem, hematoporphyrin or Sn-protoporphyrin IX to a solution of apo-ferritin crystallize in space group F432 with cell parameter a = 184.0 A. X-ray crystallographic analysis of single crystals prepared from a mixture containing haem or Sn-protoporphyrin IX shows that the haem-binding sites in these crystals are occupied by protoporphyrin IX, which is free of metal, rather than by the original metalloporphyrin. The present paper describes the structure of horse-spleen apo-ferritin cocrystallized with Sn-protoporphyrin IX. The 6797 reflections up to 2.6 A resolution used in the refinement were obtained from a data set recorded on a Nicolet/Xentronics area detector with Cu Kalpha radiation from a Rigaku RU 200 rotating anode. The final structure comprises 1613 non-H atoms, two Cd atoms and 170 solvent molecules. Four residues are described as disordered. The root-mean-square deviations from ideal bond lengths and angles are 0.013 A and 2.88 degrees, respectively. Protoporphyrins are observed in special positions on the twofold axes of the ferritin molecule with a stoichiometry of 0.4 per subunit. PubMed: 15299370DOI: 10.1107/S0907444994003227 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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