1frr: Difference between revisions

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[[Image:1frr.gif|left|200px]]


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==CRYSTAL STRUCTURE OF [2FE-2S] FERREDOXIN I FROM EQUISETUM ARVENSE AT 1.8 ANGSTROMS RESOLUTION==
The line below this paragraph, containing "STRUCTURE_1frr", creates the "Structure Box" on the page.
<StructureSection load='1frr' size='340' side='right'caption='[[1frr]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1frr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Equisetum_arvense Equisetum arvense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FRR FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr>
{{STRUCTURE_1frr| PDB=1frr |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1frr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1frr OCA], [https://pdbe.org/1frr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1frr RCSB], [https://www.ebi.ac.uk/pdbsum/1frr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1frr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FER1_EQUAR FER1_EQUAR] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fr/1frr_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1frr ConSurf].
<div style="clear:both"></div>


'''CRYSTAL STRUCTURE OF [2FE-2S] FERREDOXIN I FROM EQUISETUM ARVENSE AT 1.8 ANGSTROMS RESOLUTION'''
==See Also==
 
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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) &gt; 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 [http://en.wikipedia.org/wiki/Equisetum_arvense Equisetum arvense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FRR 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:[http://www.ncbi.nlm.nih.gov/pubmed/15299454 15299454]
[[Category: Equisetum arvense]]
[[Category: Equisetum arvense]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Tsukihara, T.]]
[[Category: Tsukihara T]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:41:25 2008''

Latest revision as of 10:18, 7 February 2024

CRYSTAL STRUCTURE OF [2FE-2S] FERREDOXIN I FROM EQUISETUM ARVENSE AT 1.8 ANGSTROMS RESOLUTIONCRYSTAL STRUCTURE OF [2FE-2S] FERREDOXIN I FROM EQUISETUM ARVENSE AT 1.8 ANGSTROMS RESOLUTION

Structural highlights

1frr is a 2 chain structure with sequence from Equisetum arvense. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FER1_EQUAR Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1frr, resolution 1.80Å

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