1isu: Difference between revisions

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THE THREE-DIMENSIONAL STRUCTURE OF THE HIGH-POTENTIAL IRON-SULFUR PROTEIN ISOLATED FROM THE PURPLE PHOTOTROPHIC BACTERIUM RHODOCYCLUS TENUIS DETERMINED AND REFINED AT 1.5 ANGSTROMS RESOLUTION

OverviewOverview

The molecular structure of the high-potential iron-sulfur protein (HiPIP) isolated from the phototrophic bacterium, Rhodocyclus tenuis, has been solved and refined to a nominal resolution of 1.5 A with a crystallographic R-factor of 17.3% for all measured X-ray data from 30 A to 1.5 A. It is the smallest of the HiPIP structures studied thus far with 62 amino acid residues. Crystals used in the investigation belonged to the space group P2(1) with unit cell dimensions of a = 36.7 A, b = 52.6 A, c = 27.6 A and beta = 90.8 degrees and contained two molecules per asymmetric unit. The structure was solved by a combination of multiple isomorphous replacement with two heavy-atom derivatives, anomalous scattering from the iron-sulfur cluster, symmetry averaging and solvent flattening. The folding motif for this HiPIP is characterized by one small alpha-helix, six Type I turns, an approximate Type II turn and one Type I' turn. As in other HiPIPs, the iron-sulfur cluster is co-ordinated by four cysteinyl ligands and exhibits a cubane-like motif. These cysteinyl ligands are all located in Type I turns. The hydrogen bonding around the metal cluster in the R. tenuis protein is similar to the patterns observed in the Chromatium vinosum and Ectothiorhodospira halophila HiPIPs. Several of the amino acid residues invariant in the previously determined C. vinosum and E. halophila structures are not retained in the R. tenuis molecule. There are 13 solvent molecules structurally conserved between the two R. tenuis HiPIP molecules in the asymmetric unit, some of which are important for stabilizing surface loops. Interestingly, while it is assumed that this HiPIP functions as a monomer in solution, the two molecules in the asymmetric unit pack as a dimer and are related to each other by an approximate twofold rotation axis.

About this StructureAbout this Structure

1ISU is a Single protein structure of sequence from Rhodocyclus tenuis with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Three-dimensional structure of the high-potential iron-sulfur protein isolated from the purple phototrophic bacterium Rhodocyclus tenuis determined and refined at 1.5 A resolution., Rayment I, Wesenberg G, Meyer TE, Cusanovich MA, Holden HM, J Mol Biol. 1992 Nov 20;228(2):672-86. PMID:1453470

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-[[Image:1isu.jpg|left|200px]]<br /><applet load="1isu" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1isu.jpg|left|200px]]<br /><applet load="1isu" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1isu, resolution 1.5&Aring;" />
 '''THE THREE-DIMENSIONAL STRUCTURE OF THE HIGH-POTENTIAL IRON-SULFUR PROTEIN ISOLATED FROM THE PURPLE PHOTOTROPHIC BACTERIUM RHODOCYCLUS TENUIS DETERMINED AND REFINED AT 1.5 ANGSTROMS RESOLUTION'''<br />
 ==Overview==
-The molecular structure of the high-potential iron-sulfur protein (HiPIP), isolated from the phototrophic bacterium, Rhodocyclus tenuis, has been, solved and refined to a nominal resolution of 1.5 A with a, crystallographic R-factor of 17.3% for all measured X-ray data from 30 A, to 1.5 A. It is the smallest of the HiPIP structures studied thus far with, 62 amino acid residues. Crystals used in the investigation belonged to the, space group P2(1) with unit cell dimensions of a = 36.7 A, b = 52.6 A, c =, 27.6 A and beta = 90.8 degrees and contained two molecules per asymmetric, unit. The structure was solved by a combination of multiple isomorphous, replacement with two heavy-atom derivatives, anomalous scattering from the, iron-sulfur cluster, symmetry averaging and solvent flattening. The, folding motif for this HiPIP is characterized by one small alpha-helix, six Type I turns, an approximate Type II turn and one Type I' turn. As in, other HiPIPs, the iron-sulfur cluster is co-ordinated by four cysteinyl, ligands and exhibits a cubane-like motif. These cysteinyl ligands are all, located in Type I turns. The hydrogen bonding around the metal cluster in, the R. tenuis protein is similar to the patterns observed in the, Chromatium vinosum and Ectothiorhodospira halophila HiPIPs. Several of the, amino acid residues invariant in the previously determined C. vinosum and, E. halophila structures are not retained in the R. tenuis molecule. There, are 13 solvent molecules structurally conserved between the two R. tenuis, HiPIP molecules in the asymmetric unit, some of which are important for, stabilizing surface loops. Interestingly, while it is assumed that this, HiPIP functions as a monomer in solution, the two molecules in the, asymmetric unit pack as a dimer and are related to each other by an, approximate twofold rotation axis.
+The molecular structure of the high-potential iron-sulfur protein (HiPIP) isolated from the phototrophic bacterium, Rhodocyclus tenuis, has been solved and refined to a nominal resolution of 1.5 A with a crystallographic R-factor of 17.3% for all measured X-ray data from 30 A to 1.5 A. It is the smallest of the HiPIP structures studied thus far with 62 amino acid residues. Crystals used in the investigation belonged to the space group P2(1) with unit cell dimensions of a = 36.7 A, b = 52.6 A, c = 27.6 A and beta = 90.8 degrees and contained two molecules per asymmetric unit. The structure was solved by a combination of multiple isomorphous replacement with two heavy-atom derivatives, anomalous scattering from the iron-sulfur cluster, symmetry averaging and solvent flattening. The folding motif for this HiPIP is characterized by one small alpha-helix, six Type I turns, an approximate Type II turn and one Type I' turn. As in other HiPIPs, the iron-sulfur cluster is co-ordinated by four cysteinyl ligands and exhibits a cubane-like motif. These cysteinyl ligands are all located in Type I turns. The hydrogen bonding around the metal cluster in the R. tenuis protein is similar to the patterns observed in the Chromatium vinosum and Ectothiorhodospira halophila HiPIPs. Several of the amino acid residues invariant in the previously determined C. vinosum and E. halophila structures are not retained in the R. tenuis molecule. There are 13 solvent molecules structurally conserved between the two R. tenuis HiPIP molecules in the asymmetric unit, some of which are important for stabilizing surface loops. Interestingly, while it is assumed that this HiPIP functions as a monomer in solution, the two molecules in the asymmetric unit pack as a dimer and are related to each other by an approximate twofold rotation axis.
 ==About this Structure==
-ISU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodocyclus_tenuis Rhodocyclus tenuis] with SF4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ISU OCA].
+ISU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodocyclus_tenuis Rhodocyclus tenuis] with <scene name='pdbligand=SF4:'>SF4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ISU OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Rhodocyclus tenuis]]
 [[Category: Single protein]]
-[[Category: Holden, H.M.]]
+[[Category: Holden, H M.]]
 [[Category: SF4]]
 [[Category: electron transfer(iron-sulfur protein)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:38:54 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:15:16 2008''