1fdn: Difference between revisions

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


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==REFINED CRYSTAL STRUCTURE OF THE 2[4FE-4S] FERREDOXIN FROM CLOSTRIDIUM ACIDURICI AT 1.84 ANGSTROMS RESOLUTION==
The line below this paragraph, containing "STRUCTURE_1fdn", creates the "Structure Box" on the page.
<StructureSection load='1fdn' size='340' side='right'caption='[[1fdn]], [[Resolution|resolution]] 1.84&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'>[[1fdn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gottschalkia_acidurici Gottschalkia acidurici]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FDN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FDN 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]] 1.84&#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=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
{{STRUCTURE_1fdn|  PDB=1fdn |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fdn OCA], [https://pdbe.org/1fdn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fdn RCSB], [https://www.ebi.ac.uk/pdbsum/1fdn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fdn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FER_GOTA9 FER_GOTA9] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.[UniProtKB:P50727]
== 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/fd/1fdn_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=1fdn ConSurf].
<div style="clear:both"></div>


'''REFINED CRYSTAL STRUCTURE OF THE 2[4FE-4S] FERREDOXIN FROM CLOSTRIDIUM ACIDURICI AT 1.84 ANGSTROMS RESOLUTION'''
==See Also==
 
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The crystal structure of the 2[4Fe-4S] ferredoxin from Clostridium acidurici has been determined at a resolution of 1.84 A and refined to an R-factor of 0.169. Crystals belong to space group P4(3)2(1)2 with unit cell dimensions a = b = 34.44 A and c = 74.78 A. The structure was determined by molecular replacement using the previously published model of an homologous ferredoxin and refined by molecular dynamics techniques. The model contains the protein and 46 water molecules. Only two amino acid residues, Asp27 and Asp28, are poorly defined in the electron density maps. The molecule has an overall chain fold similar to that of other [4Fe-4S] bacterial ferredoxins of known structure. The two [4Fe-4S] clusters display similar bond distances and angles. In both of them the co-ordination of one iron atom (bound to Cys11 and Cys40) is slightly distorted as compared with that of the other iron atoms. A core of hydrophobic residues and a few water molecules contribute to the stability of the structure. The [4Fe-4S] clusters interact with the polypeptide chain through eight hydrogen bonds each, in addition to the covalent Fe-Scys bonds. The ferredoxin from Clostridium acidurici is the most typical clostridial ferredoxin crystallized so far and the biological implications of the newly determined structure are discussed.
[[Category: Gottschalkia acidurici]]
 
[[Category: Large Structures]]
==About this Structure==
[[Category: Duee E]]
1FDN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_acidurici Clostridium acidurici]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FDN OCA].
[[Category: Fanchon E]]
 
[[Category: Meyer J]]
==Reference==
[[Category: Moulis J-M]]
Refined crystal structure of the 2[4Fe-4S] ferredoxin from Clostridium acidurici at 1.84 A resolution., Duee ED, Fanchon E, Vicat J, Sieker LC, Meyer J, Moulis JM, J Mol Biol. 1994 Nov 4;243(4):683-95. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7966291 7966291]
[[Category: Sieker LC]]
[[Category: Clostridium acidurici]]
[[Category: Vicat J]]
[[Category: Single protein]]
[[Category: Duee, E.]]
[[Category: Fanchon, E.]]
[[Category: Meyer, J.]]
[[Category: Moulis, J-M.]]
[[Category: Sieker, L C.]]
[[Category: Vicat, J.]]
[[Category: Electron transport]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:12:24 2008''

Latest revision as of 10:13, 7 February 2024

REFINED CRYSTAL STRUCTURE OF THE 2[4FE-4S] FERREDOXIN FROM CLOSTRIDIUM ACIDURICI AT 1.84 ANGSTROMS RESOLUTIONREFINED CRYSTAL STRUCTURE OF THE 2[4FE-4S] FERREDOXIN FROM CLOSTRIDIUM ACIDURICI AT 1.84 ANGSTROMS RESOLUTION

Structural highlights

1fdn is a 1 chain structure with sequence from Gottschalkia acidurici. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.84Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FER_GOTA9 Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.[UniProtKB:P50727]

Evolutionary Conservation

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

See Also

1fdn, resolution 1.84Å

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