1ier

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
==Overview==
==Overview==
-
Horse-spleen apoferritin is known to crystallize in three different space, groups, cubic F432, tetragonal P42(1)2 and orthorhombic P2(1)2(1)2. A, structure comparison of the cubic and tetragonal forms is presented here., Both crystal forms were obtained by the vapor-diffusion technique and data, were collected at 2.26 A (cubic crystal) and 2.60 A (tetragonal crystal), resolution. Two main differences were observed between these crystal, structures: (i) whereas intermolecular contacts only involve salt-bridge, type interactions via cadmium ions in the cubic structure, two types of, interactions are observed in the tetragonal crystal (cadmium-ion-mediated, salt bridges and hydrogen-bonding interactions) and (ii) cadmium ions, bound in the threefold axes of ferritin molecules exhibit lower, site-occupation factors in the tetragonal structure than in the cubic one.
+
Horse-spleen apoferritin is known to crystallize in three different space groups, cubic F432, tetragonal P42(1)2 and orthorhombic P2(1)2(1)2. A structure comparison of the cubic and tetragonal forms is presented here. Both crystal forms were obtained by the vapor-diffusion technique and data were collected at 2.26 A (cubic crystal) and 2.60 A (tetragonal crystal) resolution. Two main differences were observed between these crystal structures: (i) whereas intermolecular contacts only involve salt-bridge type interactions via cadmium ions in the cubic structure, two types of interactions are observed in the tetragonal crystal (cadmium-ion-mediated salt bridges and hydrogen-bonding interactions) and (ii) cadmium ions bound in the threefold axes of ferritin molecules exhibit lower site-occupation factors in the tetragonal structure than in the cubic one.
==About this Structure==
==About this Structure==
Line 14: Line 14:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Dautant, A.]]
[[Category: Dautant, A.]]
-
[[Category: Estaintot, B.Langlois.D.]]
+
[[Category: Estaintot, B Langlois D.]]
[[Category: Gallois, B.]]
[[Category: Gallois, B.]]
[[Category: Granier, T.]]
[[Category: Granier, T.]]
Line 23: Line 23:
[[Category: iron storage]]
[[Category: iron storage]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:50:29 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:07 2008''

Revision as of 11:11, 21 February 2008


1ier, resolution 2.26Å

Drag the structure with the mouse to rotate

CUBIC CRYSTAL STRUCTURE OF NATIVE HORSE SPLEEN FERRITIN

Overview

Horse-spleen apoferritin is known to crystallize in three different space groups, cubic F432, tetragonal P42(1)2 and orthorhombic P2(1)2(1)2. A structure comparison of the cubic and tetragonal forms is presented here. Both crystal forms were obtained by the vapor-diffusion technique and data were collected at 2.26 A (cubic crystal) and 2.60 A (tetragonal crystal) resolution. Two main differences were observed between these crystal structures: (i) whereas intermolecular contacts only involve salt-bridge type interactions via cadmium ions in the cubic structure, two types of interactions are observed in the tetragonal crystal (cadmium-ion-mediated salt bridges and hydrogen-bonding interactions) and (ii) cadmium ions bound in the threefold axes of ferritin molecules exhibit lower site-occupation factors in the tetragonal structure than in the cubic one.

About this Structure

1IER is a Single protein structure of sequence from Equus caballus with as ligand. Known structural/functional Sites: , and . Full crystallographic information is available from OCA.

Reference

Comparison of the structures of the cubic and tetragonal forms of horse-spleen apoferritin., Granier T, Gallois B, Dautant A, Langlois d'Estaintot B, Precigoux G, Acta Crystallogr D Biol Crystallogr. 1997 Sep 1;53(Pt 5):580-7. PMID:15299889

Page seeded by OCA on Thu Feb 21 13:11:07 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools