1dw3

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(New page: 200px<br /><applet load="1dw3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dw3, resolution 2.1&Aring;" /> '''STRUCTURE OF A REDUCE...)
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caption="1dw3, resolution 2.1&Aring;" />
caption="1dw3, resolution 2.1&Aring;" />
'''STRUCTURE OF A REDUCED OXYGEN BINDING CYTOCHROME C'''<br />
'''STRUCTURE OF A REDUCED OXYGEN BINDING CYTOCHROME C'''<br />
==Overview==
==Overview==
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The photosynthetic bacterium Rhodobacter sphaeroides produces a heme, protein (SHP), which is an unusual c-type cytochrome capable of, transiently binding oxygen during autooxidation. Similar proteins have not, only been observed in other photosynthetic bacteria but also in the, obligate methylotroph Methylophilus methylotrophus and the metal reducing, bacterium Shewanella putrefaciens. A three-dimensional structure of SHP, was derived using the multiple isomorphous replacement phasing method., Besides a model for the oxidized state (to 1.82 A resolution), models for, the reduced state (2.1 A resolution), the oxidized molecule liganded with, cyanide (1. 90 A resolution), and the reduced molecule liganded with, nitric oxide (2.20 A resolution) could be derived. The SHP structure, represents a new variation of the class I cytochrome c fold. The oxidized, state reveals a novel sixth heme ligand, Asn(88), which moves away from, the iron upon reduction or when small molecules bind. The distal side of, the heme has a striking resemblance to other heme proteins that bind, gaseous compounds. In SHP the liberated amide group of Asn(88) stabilizes, solvent-shielded ligands through a hydrogen bond.
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The photosynthetic bacterium Rhodobacter sphaeroides produces a heme protein (SHP), which is an unusual c-type cytochrome capable of transiently binding oxygen during autooxidation. Similar proteins have not only been observed in other photosynthetic bacteria but also in the obligate methylotroph Methylophilus methylotrophus and the metal reducing bacterium Shewanella putrefaciens. A three-dimensional structure of SHP was derived using the multiple isomorphous replacement phasing method. Besides a model for the oxidized state (to 1.82 A resolution), models for the reduced state (2.1 A resolution), the oxidized molecule liganded with cyanide (1. 90 A resolution), and the reduced molecule liganded with nitric oxide (2.20 A resolution) could be derived. The SHP structure represents a new variation of the class I cytochrome c fold. The oxidized state reveals a novel sixth heme ligand, Asn(88), which moves away from the iron upon reduction or when small molecules bind. The distal side of the heme has a striking resemblance to other heme proteins that bind gaseous compounds. In SHP the liberated amide group of Asn(88) stabilizes solvent-shielded ligands through a hydrogen bond.
==About this Structure==
==About this Structure==
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1DW3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DW3 OCA].
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1DW3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] 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=1DW3 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Backers, K.]]
[[Category: Backers, K.]]
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[[Category: Beeumen, J.J.Van.]]
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[[Category: Beeumen, J J.Van.]]
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[[Category: Cusanovich, M.A.]]
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[[Category: Cusanovich, M A.]]
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[[Category: Hagen, W.R.]]
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[[Category: Hagen, W R.]]
[[Category: Leys, D.]]
[[Category: Leys, D.]]
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[[Category: Meyer, T.E.]]
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[[Category: Meyer, T E.]]
[[Category: HEM]]
[[Category: HEM]]
[[Category: asparagine ligation]]
[[Category: asparagine ligation]]
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[[Category: reduced]]
[[Category: reduced]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:38:05 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:21:07 2008''

Revision as of 10:21, 21 February 2008


1dw3, resolution 2.1Å

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STRUCTURE OF A REDUCED OXYGEN BINDING CYTOCHROME C

Overview

The photosynthetic bacterium Rhodobacter sphaeroides produces a heme protein (SHP), which is an unusual c-type cytochrome capable of transiently binding oxygen during autooxidation. Similar proteins have not only been observed in other photosynthetic bacteria but also in the obligate methylotroph Methylophilus methylotrophus and the metal reducing bacterium Shewanella putrefaciens. A three-dimensional structure of SHP was derived using the multiple isomorphous replacement phasing method. Besides a model for the oxidized state (to 1.82 A resolution), models for the reduced state (2.1 A resolution), the oxidized molecule liganded with cyanide (1. 90 A resolution), and the reduced molecule liganded with nitric oxide (2.20 A resolution) could be derived. The SHP structure represents a new variation of the class I cytochrome c fold. The oxidized state reveals a novel sixth heme ligand, Asn(88), which moves away from the iron upon reduction or when small molecules bind. The distal side of the heme has a striking resemblance to other heme proteins that bind gaseous compounds. In SHP the liberated amide group of Asn(88) stabilizes solvent-shielded ligands through a hydrogen bond.

About this Structure

1DW3 is a Single protein structure of sequence from Rhodobacter sphaeroides with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structures of an oxygen-binding cytochrome c from Rhodobacter sphaeroides., Leys D, Backers K, Meyer TE, Hagen WR, Cusanovich MA, Van Beeumen JJ, J Biol Chem. 2000 May 26;275(21):16050-6. PMID:10821858

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