1fxd: Difference between revisions

Line 1:

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

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

caption="1fxd, resolution 1.7Å" />

'''REFINED CRYSTAL STRUCTURE OF FERREDOXIN II FROM DESULFOVIBRIO GIGAS AT 1.7 ANGSTROMS'''<br />

==Overview==

The crystal structure of ferredoxin II from Desulfovibrio gigas has been, determined using phasing from anomalous scattering data at a resolution of, 1.7 A and refined to an R-factor of 0.157. The molecule has an overall, chain fold similar to that of the other bacterial ferredoxins of known, structure. The molecule contains a single 3Fe-4S cluster with geometry, indistinguishable from the 4Fe-4S clusters, and a disulfide bond near the, site corresponding to the position of the second cluster of two-cluster, ferredoxins. The cluster is bound by cysteine residues 8, 14 and 50. The, side-chain of cysteine 11 extends away from the cluster, but could rotate, to become the fourth cysteine ligand in the four-iron form of the molecule, given a local adjustment of the polypeptide chain. This residue is, modified, however, by what appears to be a methanethiol group. There are a, total of eight NH . . . S bonds to the inorganic and cysteine sulfur atoms, of the Fe-S cluster. There is an additional residue found that is not, reported for the chemical sequence: according to the electron density a, valine residue should be inserted after residue 55.

The crystal structure of ferredoxin II from Desulfovibrio gigas has been determined using phasing from anomalous scattering data at a resolution of 1.7 A and refined to an R-factor of 0.157. The molecule has an overall chain fold similar to that of the other bacterial ferredoxins of known structure. The molecule contains a single 3Fe-4S cluster with geometry indistinguishable from the 4Fe-4S clusters, and a disulfide bond near the site corresponding to the position of the second cluster of two-cluster ferredoxins. The cluster is bound by cysteine residues 8, 14 and 50. The side-chain of cysteine 11 extends away from the cluster, but could rotate to become the fourth cysteine ligand in the four-iron form of the molecule given a local adjustment of the polypeptide chain. This residue is modified, however, by what appears to be a methanethiol group. There are a total of eight NH . . . S bonds to the inorganic and cysteine sulfur atoms of the Fe-S cluster. There is an additional residue found that is not reported for the chemical sequence: according to the electron density a valine residue should be inserted after residue 55.

==About this Structure==

1FXD 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 F3S as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1FXD OCA].

1FXD 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=F3S:'>F3S</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FXD OCA].

==Reference==

Line 13:

[[Category: Desulfovibrio gigas]]

[[Category: Single protein]]

[[Category: Adman, E.T.]]

[[Category: Adman, E T.]]

[[Category: Jensen, L.H.]]

[[Category: Jensen, L H.]]

[[Category: Kissinger, C.R.]]

[[Category: Kissinger, C R.]]

[[Category: Sieker, L.C.]]

[[Category: Sieker, L C.]]

[[Category: F3S]]

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

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 15~~:25:~~58 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:38 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1fxd.gif|left|200px]]<br /><applet load="1fxd" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1fxd.gif|left|200px]]<br /><applet load="1fxd" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1fxd, resolution 1.7&Aring;" />
 '''REFINED CRYSTAL STRUCTURE OF FERREDOXIN II FROM DESULFOVIBRIO GIGAS AT 1.7 ANGSTROMS'''<br />
 ==Overview==
-The crystal structure of ferredoxin II from Desulfovibrio gigas has been, determined using phasing from anomalous scattering data at a resolution of, 1.7 A and refined to an R-factor of 0.157. The molecule has an overall, chain fold similar to that of the other bacterial ferredoxins of known, structure. The molecule contains a single 3Fe-4S cluster with geometry, indistinguishable from the 4Fe-4S clusters, and a disulfide bond near the, site corresponding to the position of the second cluster of two-cluster, ferredoxins. The cluster is bound by cysteine residues 8, 14 and 50. The, side-chain of cysteine 11 extends away from the cluster, but could rotate, to become the fourth cysteine ligand in the four-iron form of the molecule, given a local adjustment of the polypeptide chain. This residue is, modified, however, by what appears to be a methanethiol group. There are a, total of eight NH . . . S bonds to the inorganic and cysteine sulfur atoms, of the Fe-S cluster. There is an additional residue found that is not, reported for the chemical sequence: according to the electron density a, valine residue should be inserted after residue 55.
+The crystal structure of ferredoxin II from Desulfovibrio gigas has been determined using phasing from anomalous scattering data at a resolution of 1.7 A and refined to an R-factor of 0.157. The molecule has an overall chain fold similar to that of the other bacterial ferredoxins of known structure. The molecule contains a single 3Fe-4S cluster with geometry indistinguishable from the 4Fe-4S clusters, and a disulfide bond near the site corresponding to the position of the second cluster of two-cluster ferredoxins. The cluster is bound by cysteine residues 8, 14 and 50. The side-chain of cysteine 11 extends away from the cluster, but could rotate to become the fourth cysteine ligand in the four-iron form of the molecule given a local adjustment of the polypeptide chain. This residue is modified, however, by what appears to be a methanethiol group. There are a total of eight NH . . . S bonds to the inorganic and cysteine sulfur atoms of the Fe-S cluster. There is an additional residue found that is not reported for the chemical sequence: according to the electron density a valine residue should be inserted after residue 55.
 ==About this Structure==
-FXD 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 F3S as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FXD OCA].
+FXD 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=F3S:'>F3S</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FXD OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Desulfovibrio gigas]]
 [[Category: Single protein]]
-[[Category: Adman, E.T.]]
+[[Category: Adman, E T.]]
-[[Category: Jensen, L.H.]]
+[[Category: Jensen, L H.]]
-[[Category: Kissinger, C.R.]]
+[[Category: Kissinger, C R.]]
-[[Category: Sieker, L.C.]]
+[[Category: Sieker, L C.]]
 [[Category: F3S]]
 [[Category: electron transfer(iron-sulfur)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:25:58 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:38 2008''