1frr
From Proteopedia
(New page: 200px<br /><applet load="1frr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1frr, resolution 1.8Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1frr.gif|left|200px]]<br /><applet load="1frr" size=" | + | [[Image:1frr.gif|left|200px]]<br /><applet load="1frr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1frr, resolution 1.8Å" /> | caption="1frr, resolution 1.8Å" /> | ||
'''CRYSTAL STRUCTURE OF [2FE-2S] FERREDOXIN I FROM EQUISETUM ARVENSE AT 1.8 ANGSTROMS RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF [2FE-2S] FERREDOXIN I FROM EQUISETUM ARVENSE AT 1.8 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Ferredoxin I (Fd I) from Equisetum arvense is an iron-sulfur protein | + | Ferredoxin I (Fd I) from Equisetum arvense is an iron-sulfur protein composed of 95 amino-acid residues and one [2Fe-2S] cluster. It crystallized in the space group P2(1), a = 30.4, b = 57.4, c = 47.5 A and beta = 78.7 degrees with two molecules per asymmetric unit. X-ray diffraction data up to 1.8 A resolution were collected by using a Rigaku four-circle diffractometer. The initial model of Fd I, which was derived by the molecular replacement method using a structure of the Fd I from the blue-green alga Aphanothece sacrum, was refined by molecular dynamics simulation and a least-squares minimization with stereochemical restraints. Positional parameters and isotropic temperature factors for 1420 non-H protein atoms and 183 water molecules were refined on 13 838 observed structure factors (F(o) > sigma(Fo)) between 10.0 and 1.8 A resolution. The final Rfactor was 17.0%, and the standard deviation of atomic position estimated by Luzzati plot [Luzzati (1952). Acta Cryst. 5, 802-810] was 0.2 A. The electron-density map was well defined for the two independent molecules except for the N-terminal residue and the three C-terminal residues. Equivalent Calpha atoms of two independent molecules in the asymmetric unit were superposed by the least-squares method with root-mean-square deviations of 0.26 A. Reasonable structural differences were observed at a polypeptide segment having few intramolecular interactions. Highly flexible regions of the molecule were assigned from the structural differences between the two independent molecules in the crystal and the distribution of temperature factors along the polypeptide chain. |
==About this Structure== | ==About this Structure== | ||
| - | 1FRR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equisetum_arvense Equisetum arvense] with FES as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1FRR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equisetum_arvense Equisetum arvense] 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=1FRR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: electron transfer(iron-sulfur protein)]] | [[Category: electron transfer(iron-sulfur protein)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:41:56 2008'' |
Revision as of 10:41, 21 February 2008
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CRYSTAL STRUCTURE OF [2FE-2S] FERREDOXIN I FROM EQUISETUM ARVENSE AT 1.8 ANGSTROMS RESOLUTION
Overview
Ferredoxin I (Fd I) from Equisetum arvense is an iron-sulfur protein composed of 95 amino-acid residues and one [2Fe-2S] cluster. It crystallized in the space group P2(1), a = 30.4, b = 57.4, c = 47.5 A and beta = 78.7 degrees with two molecules per asymmetric unit. X-ray diffraction data up to 1.8 A resolution were collected by using a Rigaku four-circle diffractometer. The initial model of Fd I, which was derived by the molecular replacement method using a structure of the Fd I from the blue-green alga Aphanothece sacrum, was refined by molecular dynamics simulation and a least-squares minimization with stereochemical restraints. Positional parameters and isotropic temperature factors for 1420 non-H protein atoms and 183 water molecules were refined on 13 838 observed structure factors (F(o) > sigma(Fo)) between 10.0 and 1.8 A resolution. The final Rfactor was 17.0%, and the standard deviation of atomic position estimated by Luzzati plot [Luzzati (1952). Acta Cryst. 5, 802-810] was 0.2 A. The electron-density map was well defined for the two independent molecules except for the N-terminal residue and the three C-terminal residues. Equivalent Calpha atoms of two independent molecules in the asymmetric unit were superposed by the least-squares method with root-mean-square deviations of 0.26 A. Reasonable structural differences were observed at a polypeptide segment having few intramolecular interactions. Highly flexible regions of the molecule were assigned from the structural differences between the two independent molecules in the crystal and the distribution of temperature factors along the polypeptide chain.
About this Structure
1FRR is a Single protein structure of sequence from Equisetum arvense with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of [2Fe-2S] ferredoxin I from Equisetum arvense at 1.8 A resolution., Ikemizu S, Bando M, Sato T, Morimoto Y, Tsukihara T, Fukuyama K, Acta Crystallogr D Biol Crystallogr. 1994 Mar 1;50(Pt 2):167-74. PMID:15299454
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