1ryt

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(New page: 200px<br /><applet load="1ryt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ryt, resolution 2.1&Aring;" /> '''RUBRERYTHRIN'''<br />...)
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'''RUBRERYTHRIN'''<br />
'''RUBRERYTHRIN'''<br />
==Overview==
==Overview==
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We have determined the structure of rubrerythrin, a non-haem iron protein, from the anaerobic sulphate-reducing bacterium, Desulfovibrio vulgaris, (Hildenborough), by X-ray crystallography. The structure reveals a, tetramer of two-domain subunits. Each subunit contains a four-helix bundle, surrounding a diiron-oxo site and a C-terminal rubredoxin-like FeS4, domain. The diiron-oxo site contains a larger number of carboxylate, ligands and a higher degree of solvent exposure than do those in other, diiron-oxo proteins. The four-helix bundle of rubrerythrin closely, resembles those of the ferritin and bacterioferritin subunits, suggesting, a relationship among these proteins-consistent with the recently, demonstrated ferroxidase activity of rubrerythrin.
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We have determined the structure of rubrerythrin, a non-haem iron protein from the anaerobic sulphate-reducing bacterium, Desulfovibrio vulgaris (Hildenborough), by X-ray crystallography. The structure reveals a tetramer of two-domain subunits. Each subunit contains a four-helix bundle surrounding a diiron-oxo site and a C-terminal rubredoxin-like FeS4 domain. The diiron-oxo site contains a larger number of carboxylate ligands and a higher degree of solvent exposure than do those in other diiron-oxo proteins. The four-helix bundle of rubrerythrin closely resembles those of the ferritin and bacterioferritin subunits, suggesting a relationship among these proteins-consistent with the recently demonstrated ferroxidase activity of rubrerythrin.
==About this Structure==
==About this Structure==
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1RYT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris] with FE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RYT OCA].
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1RYT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris] with <scene name='pdbligand=FE:'>FE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RYT OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Demare, F.]]
[[Category: Demare, F.]]
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[[Category: Kurtz, D.M.]]
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[[Category: Kurtz, D M.]]
[[Category: Nordlund, P.]]
[[Category: Nordlund, P.]]
[[Category: FE]]
[[Category: FE]]
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[[Category: iron]]
[[Category: iron]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:58:18 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:56:07 2008''

Revision as of 12:56, 21 February 2008


1ryt, resolution 2.1Å

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RUBRERYTHRIN

Overview

We have determined the structure of rubrerythrin, a non-haem iron protein from the anaerobic sulphate-reducing bacterium, Desulfovibrio vulgaris (Hildenborough), by X-ray crystallography. The structure reveals a tetramer of two-domain subunits. Each subunit contains a four-helix bundle surrounding a diiron-oxo site and a C-terminal rubredoxin-like FeS4 domain. The diiron-oxo site contains a larger number of carboxylate ligands and a higher degree of solvent exposure than do those in other diiron-oxo proteins. The four-helix bundle of rubrerythrin closely resembles those of the ferritin and bacterioferritin subunits, suggesting a relationship among these proteins-consistent with the recently demonstrated ferroxidase activity of rubrerythrin.

About this Structure

1RYT is a Single protein structure of sequence from Desulfovibrio vulgaris with as ligand. Full crystallographic information is available from OCA.

Reference

The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains., deMare F, Kurtz DM Jr, Nordlund P, Nat Struct Biol. 1996 Jun;3(6):539-46. PMID:8646540

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