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1hrs
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(New page: 200px<br /><applet load="1hrs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hrs, resolution 2.6Å" /> '''A CRYSTALLOGRAPHIC ST...)
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Revision as of 14:40, 20 November 2007
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A CRYSTALLOGRAPHIC STUDY OF HAEM BINDING TO FERRITIN
Overview
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.
About this Structure
1HRS is a Single protein structure of sequence from Equus caballus with CD and PP9 as ligands. Full crystallographic information is available from OCA.
Reference
A crystallographic study of haem binding to ferritin., Precigoux G, Yariv J, Gallois B, Courseille C, d'Estaintot BL, Acta Crystallogr D Biol Crystallogr. 1994 Sep 1;50(Pt 5):739-43. PMID:15299370
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