1jgc
From Proteopedia
(New page: 200px<br /><applet load="1jgc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jgc, resolution 2.60Å" /> '''The 2.6 A Structure ...) |
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| - | [[Image:1jgc.gif|left|200px]]<br /><applet load="1jgc" size=" | + | [[Image:1jgc.gif|left|200px]]<br /><applet load="1jgc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jgc, resolution 2.60Å" /> | caption="1jgc, resolution 2.60Å" /> | ||
'''The 2.6 A Structure Resolution of Rhodobacter capsulatus Bacterioferritin with Metal-free Dinuclear Site and Heme Iron in a Crystallographic Special Position'''<br /> | '''The 2.6 A Structure Resolution of Rhodobacter capsulatus Bacterioferritin with Metal-free Dinuclear Site and Heme Iron in a Crystallographic Special Position'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bacterioferritin from Rhodobacter capsulatus was crystallized and its | + | Bacterioferritin from Rhodobacter capsulatus was crystallized and its structure was solved at 2.6 A resolution. This first structure of a bacterioferritin from a photosynthetic organism is a spherical particle of 24 subunits displaying 432 point-group symmetry like ferritin and bacterioferritin from Escherichia coli. Crystallized in the I422 space group, its structural analysis reveals for the first time the non-symmetric heme molecule located on a twofold crystallographic symmetry axis. Other hemes of the protomer are situated on twofold noncrystallographic axes. Apparently, both types of sites bind heme in two orientations, leading to an average structure consisting of a symmetric 50:50 mixture, thus satisfying the crystallographic and noncrystallographic symmetry of the crystal. Five water molecules are situated close to the heme, which is bound in a hydrophobic pocket and axially coordinated by two crystallographic or noncrystallographically related methionine residues. Its ferroxidase center, in which Fe(II) is oxidized to Fe(III), is empty or fractionally occupied by a metal ion. Two positions are observed for the coordinating Glu18 side chain instead of one in the E. coli enzyme in which the site is occupied. This result suggests that the orientation of the Glu18 side chain could be constrained by this interaction. |
==About this Structure== | ==About this Structure== | ||
| - | 1JGC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1JGC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JGC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ban, M.]] | [[Category: Ban, M.]] | ||
| - | [[Category: Berry, E | + | [[Category: Berry, E A.]] |
[[Category: Cobessi, D.]] | [[Category: Cobessi, D.]] | ||
[[Category: Daldal, F.]] | [[Category: Daldal, F.]] | ||
| - | [[Category: Huang, L | + | [[Category: Huang, L S.]] |
| - | [[Category: Pon, N | + | [[Category: Pon, N G.]] |
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: iron storage protein]] | [[Category: iron storage protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:22:21 2008'' |
Revision as of 11:22, 21 February 2008
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The 2.6 A Structure Resolution of Rhodobacter capsulatus Bacterioferritin with Metal-free Dinuclear Site and Heme Iron in a Crystallographic Special Position
Overview
Bacterioferritin from Rhodobacter capsulatus was crystallized and its structure was solved at 2.6 A resolution. This first structure of a bacterioferritin from a photosynthetic organism is a spherical particle of 24 subunits displaying 432 point-group symmetry like ferritin and bacterioferritin from Escherichia coli. Crystallized in the I422 space group, its structural analysis reveals for the first time the non-symmetric heme molecule located on a twofold crystallographic symmetry axis. Other hemes of the protomer are situated on twofold noncrystallographic axes. Apparently, both types of sites bind heme in two orientations, leading to an average structure consisting of a symmetric 50:50 mixture, thus satisfying the crystallographic and noncrystallographic symmetry of the crystal. Five water molecules are situated close to the heme, which is bound in a hydrophobic pocket and axially coordinated by two crystallographic or noncrystallographically related methionine residues. Its ferroxidase center, in which Fe(II) is oxidized to Fe(III), is empty or fractionally occupied by a metal ion. Two positions are observed for the coordinating Glu18 side chain instead of one in the E. coli enzyme in which the site is occupied. This result suggests that the orientation of the Glu18 side chain could be constrained by this interaction.
About this Structure
1JGC is a Single protein structure of sequence from Rhodobacter capsulatus with as ligand. Full crystallographic information is available from OCA.
Reference
The 2.6 A resolution structure of Rhodobacter capsulatus bacterioferritin with metal-free dinuclear site and heme iron in a crystallographic 'special position'., Cobessi D, Huang LS, Ban M, Pon NG, Daldal F, Berry EA, Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):29-38. Epub 2001, Dec 21. PMID:11752777
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