2dsx: Difference between revisions

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Crystal structure of rubredoxin from Desulfovibrio gigas to ultra-high 0.68 A resolution

OverviewOverview

Rubredoxin (D.g. Rd) is a small non-heme iron-sulfur protein shown to function as a redox coupling protein from the sulfate reducing bacteria Desulfovibrio gigas. The protein is generally purified from anaerobic bacteria in which it is thought to be involved in electron transfer or exchange processes. Rd transfers an electron to oxygen to form water as part of a unique electron transfer chain, composed by NADH:rubredoxin oxidoreductase (NRO), rubredoxin and rubredoxin:oxygen oxidoreductase (ROO) in D.g. The crystal structure of D.g. Rd has been determined by means of both a Fe single-wavelength anomalous dispersion (SAD) signal and the direct method, and refined to an ultra-high 0.68 A resolution, using X-ray from a synchrotron. Rd contains one iron atom bound in a tetrahedral coordination by the sulfur atoms of four cysteinyl residues. Hydrophobic and pi-pi interactions maintain the internal Rd folding. Multiple conformations of the iron-sulfur cluster and amino acid residues are observed and indicate its unique mechanism of electron transfer. Several hydrogen bonds, including N-H...SG of the iron-sulfur, are revealed clearly in maps of electron density. Abundant waters bound to C-O peptides of residues Val8, Cys9, Gly10, Ala38, and Gly43, which may be involved in electron transfer. This ultrahigh-resolution structure allows us to study in great detail the relationship between structure and function of rubredoxin, such as salt bridges, hydrogen bonds, water structures, cysteine ligands, iron-sulfur cluster, and distributions of electron density among activity sites. For the first time, this information will provide a clear role for this protein in a strict anaerobic bacterium.

About this StructureAbout this Structure

2DSX is a Single protein structure of sequence from Desulfovibrio gigas with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of rubredoxin from Desulfovibrio gigas to ultra-high 0.68 A resolution., Chen CJ, Lin YH, Huang YC, Liu MY, Biochem Biophys Res Commun. 2006 Oct 13;349(1):79-90. Epub 2006 Aug 11. PMID:16930541

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-[[Image:2dsx.gif|left|200px]]<br /><applet load="2dsx" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="2dsx, resolution 0.68&Aring;" />
 '''Crystal structure of rubredoxin from Desulfovibrio gigas to ultra-high 0.68 A resolution'''<br />
 ==Overview==
-Rubredoxin (D.g. Rd) is a small non-heme iron-sulfur protein shown to, function as a redox coupling protein from the sulfate reducing bacteria, Desulfovibrio gigas. The protein is generally purified from anaerobic, bacteria in which it is thought to be involved in electron transfer or, exchange processes. Rd transfers an electron to oxygen to form water as, part of a unique electron transfer chain, composed by NADH:rubredoxin, oxidoreductase (NRO), rubredoxin and rubredoxin:oxygen oxidoreductase, (ROO) in D.g. The crystal structure of D.g. Rd has been determined by, means of both a Fe single-wavelength anomalous dispersion (SAD) signal and, the direct method, and refined to an ultra-high 0.68 A resolution, using, X-ray from a synchrotron. Rd contains one iron atom bound in a tetrahedral, coordination by the sulfur atoms of four cysteinyl residues. Hydrophobic, and pi-pi interactions maintain the internal Rd folding. Multiple, conformations of the iron-sulfur cluster and amino acid residues are, observed and indicate its unique mechanism of electron transfer. Several, hydrogen bonds, including N-H...SG of the iron-sulfur, are revealed, clearly in maps of electron density. Abundant waters bound to C-O peptides, of residues Val8, Cys9, Gly10, Ala38, and Gly43, which may be involved in, electron transfer. This ultrahigh-resolution structure allows us to study, in great detail the relationship between structure and function of, rubredoxin, such as salt bridges, hydrogen bonds, water structures, cysteine ligands, iron-sulfur cluster, and distributions of electron, density among activity sites. For the first time, this information will, provide a clear role for this protein in a strict anaerobic bacterium.
+Rubredoxin (D.g. Rd) is a small non-heme iron-sulfur protein shown to function as a redox coupling protein from the sulfate reducing bacteria Desulfovibrio gigas. The protein is generally purified from anaerobic bacteria in which it is thought to be involved in electron transfer or exchange processes. Rd transfers an electron to oxygen to form water as part of a unique electron transfer chain, composed by NADH:rubredoxin oxidoreductase (NRO), rubredoxin and rubredoxin:oxygen oxidoreductase (ROO) in D.g. The crystal structure of D.g. Rd has been determined by means of both a Fe single-wavelength anomalous dispersion (SAD) signal and the direct method, and refined to an ultra-high 0.68 A resolution, using X-ray from a synchrotron. Rd contains one iron atom bound in a tetrahedral coordination by the sulfur atoms of four cysteinyl residues. Hydrophobic and pi-pi interactions maintain the internal Rd folding. Multiple conformations of the iron-sulfur cluster and amino acid residues are observed and indicate its unique mechanism of electron transfer. Several hydrogen bonds, including N-H...SG of the iron-sulfur, are revealed clearly in maps of electron density. Abundant waters bound to C-O peptides of residues Val8, Cys9, Gly10, Ala38, and Gly43, which may be involved in electron transfer. This ultrahigh-resolution structure allows us to study in great detail the relationship between structure and function of rubredoxin, such as salt bridges, hydrogen bonds, water structures, cysteine ligands, iron-sulfur cluster, and distributions of electron density among activity sites. For the first time, this information will provide a clear role for this protein in a strict anaerobic bacterium.
 ==About this Structure==
-DSX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_gigas Desulfovibrio gigas] 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=2DSX OCA].
+DSX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_gigas Desulfovibrio gigas] 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=2DSX OCA].
 ==Reference==
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 [[Category: Desulfovibrio gigas]]
 [[Category: Single protein]]
-[[Category: Chen, C.J.]]
+[[Category: Chen, C J.]]
-[[Category: Huang, Y.C.]]
+[[Category: Huang, Y C.]]
-[[Category: Lin, Y.H.]]
+[[Category: Lin, Y H.]]
-[[Category: Liu, M.Y.]]
+[[Category: Liu, M Y.]]
 [[Category: FE]]
 [[Category: desulfovibrio gigas]]
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 [[Category: rubredoxin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:45:58 2007''
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