1fxi: Difference between revisions

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[[Image:1fxi.gif|left|200px]]<br /><applet load="1fxi" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1fxi.gif|left|200px]]<br /><applet load="1fxi" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1fxi, resolution 2.2Å" />

'''STRUCTURE OF THE [2FE-2S] FERREDOXIN I FROM THE BLUE-GREEN ALGA APHANOTHECE SACRUM AT 2.2 ANGSTROMS RESOLUTION'''<br />

==Overview==

Crystals of a [2Fe-2S] ferredoxin (Fd) I with a relative molecular mass of, 10,480 were obtained from the blue-green alga Aphanothece sacrum. Each, asymmetric unit of the crystal contains four molecules. An electron, density map calculated by the single isomorphous replacement method with, the anomalous dispersion at 2.5 A resolution was refined by averaging the, four molecules in the asymmetric unit. Positional and isotropic thermal, parameters for the non-hydrogen atoms of the four molecules and 158 water, molecules were refined to an R-factor (R = sigma[Fo-Fc[/sigma Fo) of 0.23, by the restrained least-squares method. The estimated root-mean-square, (r.m.s.) error for the atomic positions is 0.3 A. The r.m.s. deviations of, equivalent C alpha atoms of the asymmetric-unit molecules superposed by, the least-squares method average 0.35 A. The Fd molecule has a structure, like the beta-barrel in the molecule of the [2Fe-2S] Fd from Spirulina, platensis. A [2Fe-2S] cluster is bonded covalently to the protein molecule, by four Fe-S, in which three of the Fe-S bonds are in a loop segment from, position 38 to 47. The hydrophobic core inside the beta-barrel is formed, by seven conservative residues: Val15, Val18, Ile24, Leu51, Ile74, Ala79, and Ile87. The molecular surface around Tyr23, Tyr80 and the active center, may interact with ferredoxin-NADP+ reductase. One of the two iron atoms of, the [2Fe-2S] cluster should be more easily reduced than the other because, of differences in the hydrogen-bonding scheme and the hydrophobicity, around the atoms.

Crystals of a [2Fe-2S] ferredoxin (Fd) I with a relative molecular mass of 10,480 were obtained from the blue-green alga Aphanothece sacrum. Each asymmetric unit of the crystal contains four molecules. An electron density map calculated by the single isomorphous replacement method with the anomalous dispersion at 2.5 A resolution was refined by averaging the four molecules in the asymmetric unit. Positional and isotropic thermal parameters for the non-hydrogen atoms of the four molecules and 158 water molecules were refined to an R-factor (R = sigma[Fo-Fc[/sigma Fo) of 0.23 by the restrained least-squares method. The estimated root-mean-square (r.m.s.) error for the atomic positions is 0.3 A. The r.m.s. deviations of equivalent C alpha atoms of the asymmetric-unit molecules superposed by the least-squares method average 0.35 A. The Fd molecule has a structure like the beta-barrel in the molecule of the [2Fe-2S] Fd from Spirulina platensis. A [2Fe-2S] cluster is bonded covalently to the protein molecule by four Fe-S, in which three of the Fe-S bonds are in a loop segment from position 38 to 47. The hydrophobic core inside the beta-barrel is formed by seven conservative residues: Val15, Val18, Ile24, Leu51, Ile74, Ala79 and Ile87. The molecular surface around Tyr23, Tyr80 and the active center may interact with ferredoxin-NADP+ reductase. One of the two iron atoms of the [2Fe-2S] cluster should be more easily reduced than the other because of differences in the hydrogen-bonding scheme and the hydrophobicity around the atoms.

==About this Structure==

1FXI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aphanothece_sacrum Aphanothece sacrum] with FES as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1FXI OCA].

1FXI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aphanothece_sacrum Aphanothece sacrum] with <scene name='pdbligand=FES:'>FES</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FXI OCA].

==Reference==

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[[Category: electron transfer (iron-sulfur protein)]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 15~~:26:~~12 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:39 2008''

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-[[Image:1fxi.gif|left|200px]]<br /><applet load="1fxi" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1fxi.gif|left|200px]]<br /><applet load="1fxi" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1fxi, resolution 2.2&Aring;" />
 '''STRUCTURE OF THE [2FE-2S] FERREDOXIN I FROM THE BLUE-GREEN ALGA APHANOTHECE SACRUM AT 2.2 ANGSTROMS RESOLUTION'''<br />
 ==Overview==
-Crystals of a [2Fe-2S] ferredoxin (Fd) I with a relative molecular mass of, 10,480 were obtained from the blue-green alga Aphanothece sacrum. Each, asymmetric unit of the crystal contains four molecules. An electron, density map calculated by the single isomorphous replacement method with, the anomalous dispersion at 2.5 A resolution was refined by averaging the, four molecules in the asymmetric unit. Positional and isotropic thermal, parameters for the non-hydrogen atoms of the four molecules and 158 water, molecules were refined to an R-factor (R = sigma[Fo-Fc[/sigma Fo) of 0.23, by the restrained least-squares method. The estimated root-mean-square, (r.m.s.) error for the atomic positions is 0.3 A. The r.m.s. deviations of, equivalent C alpha atoms of the asymmetric-unit molecules superposed by, the least-squares method average 0.35 A. The Fd molecule has a structure, like the beta-barrel in the molecule of the [2Fe-2S] Fd from Spirulina, platensis. A [2Fe-2S] cluster is bonded covalently to the protein molecule, by four Fe-S, in which three of the Fe-S bonds are in a loop segment from, position 38 to 47. The hydrophobic core inside the beta-barrel is formed, by seven conservative residues: Val15, Val18, Ile24, Leu51, Ile74, Ala79, and Ile87. The molecular surface around Tyr23, Tyr80 and the active center, may interact with ferredoxin-NADP+ reductase. One of the two iron atoms of, the [2Fe-2S] cluster should be more easily reduced than the other because, of differences in the hydrogen-bonding scheme and the hydrophobicity, around the atoms.
+Crystals of a [2Fe-2S] ferredoxin (Fd) I with a relative molecular mass of 10,480 were obtained from the blue-green alga Aphanothece sacrum. Each asymmetric unit of the crystal contains four molecules. An electron density map calculated by the single isomorphous replacement method with the anomalous dispersion at 2.5 A resolution was refined by averaging the four molecules in the asymmetric unit. Positional and isotropic thermal parameters for the non-hydrogen atoms of the four molecules and 158 water molecules were refined to an R-factor (R = sigma[Fo-Fc[/sigma Fo) of 0.23 by the restrained least-squares method. The estimated root-mean-square (r.m.s.) error for the atomic positions is 0.3 A. The r.m.s. deviations of equivalent C alpha atoms of the asymmetric-unit molecules superposed by the least-squares method average 0.35 A. The Fd molecule has a structure like the beta-barrel in the molecule of the [2Fe-2S] Fd from Spirulina platensis. A [2Fe-2S] cluster is bonded covalently to the protein molecule by four Fe-S, in which three of the Fe-S bonds are in a loop segment from position 38 to 47. The hydrophobic core inside the beta-barrel is formed by seven conservative residues: Val15, Val18, Ile24, Leu51, Ile74, Ala79 and Ile87. The molecular surface around Tyr23, Tyr80 and the active center may interact with ferredoxin-NADP+ reductase. One of the two iron atoms of the [2Fe-2S] cluster should be more easily reduced than the other because of differences in the hydrogen-bonding scheme and the hydrophobicity around the atoms.
 ==About this Structure==
-FXI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aphanothece_sacrum Aphanothece sacrum] with FES as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FXI OCA].
+FXI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aphanothece_sacrum Aphanothece sacrum] with <scene name='pdbligand=FES:'>FES</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FXI OCA].
 ==Reference==
@@ Line 17: / Line 17: @@
 [[Category: electron transfer (iron-sulfur protein)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:26:12 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:39 2008''