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1hrs
From Proteopedia
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| - | [[Image:1hrs.gif|left|200px]] | + | [[Image:1hrs.gif|left|200px]] |
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| - | '''A CRYSTALLOGRAPHIC STUDY OF HAEM BINDING TO FERRITIN''' | + | {{Structure |
| + | |PDB= 1hrs |SIZE=350|CAPTION= <scene name='initialview01'>1hrs</scene>, resolution 2.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> and <scene name='pdbligand=PP9:PROTOPORPHYRIN IX'>PP9</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''A CRYSTALLOGRAPHIC STUDY OF HAEM BINDING TO FERRITIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HRS is a [ | + | 1HRS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRS OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15299370 15299370] |
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: iron storage]] | [[Category: iron storage]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:40:58 2008'' |
Revision as of 09:40, 20 March 2008
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| , resolution 2.6Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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