1hrs
From Proteopedia
(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...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1hrs.gif|left|200px]]<br /><applet load="1hrs" size=" | + | [[Image:1hrs.gif|left|200px]]<br /><applet load="1hrs" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hrs, resolution 2.6Å" /> | caption="1hrs, resolution 2.6Å" /> | ||
'''A CRYSTALLOGRAPHIC STUDY OF HAEM BINDING TO FERRITIN'''<br /> | '''A CRYSTALLOGRAPHIC STUDY OF HAEM BINDING TO FERRITIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Ferritin, the iron-storage protein, binds porphyrins, metalloporphyrins | + | 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== | ==About this Structure== | ||
| - | 1HRS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with CD and PP9 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1HRS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with <scene name='pdbligand=CD:'>CD</scene> and <scene name='pdbligand=PP9:'>PP9</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRS OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Courseille, C.]] | [[Category: Courseille, C.]] | ||
[[Category: Dautant, A.]] | [[Category: Dautant, A.]] | ||
| - | [[Category: Estaintot, B | + | [[Category: Estaintot, B Langlois D.]] |
[[Category: Gallois, B.]] | [[Category: Gallois, B.]] | ||
[[Category: Precigoux, G.]] | [[Category: Precigoux, G.]] | ||
| Line 23: | Line 23: | ||
[[Category: iron storage]] | [[Category: iron storage]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:14 2008'' |
Revision as of 11:04, 21 February 2008
|
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 and 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
Page seeded by OCA on Thu Feb 21 13:04:14 2008
