1fdn: Difference between revisions
New page: left|200px<br /><applet load="1fdn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fdn, resolution 1.84Å" /> '''REFINED CRYSTAL STRU... |
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[[Image:1fdn.gif|left|200px]]<br /><applet load="1fdn" size=" | [[Image:1fdn.gif|left|200px]]<br /><applet load="1fdn" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1fdn, resolution 1.84Å" /> | caption="1fdn, resolution 1.84Å" /> | ||
'''REFINED CRYSTAL STRUCTURE OF THE 2[4FE-4S] FERREDOXIN FROM CLOSTRIDIUM ACIDURICI AT 1.84 ANGSTROMS RESOLUTION'''<br /> | '''REFINED CRYSTAL STRUCTURE OF THE 2[4FE-4S] FERREDOXIN FROM CLOSTRIDIUM ACIDURICI AT 1.84 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of the 2[4Fe-4S] ferredoxin from Clostridium | 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. | ||
==About this Structure== | ==About this Structure== | ||
1FDN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_acidurici Clostridium acidurici] with SF4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1FDN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_acidurici Clostridium acidurici] 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=1FDN OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Meyer, J.]] | [[Category: Meyer, J.]] | ||
[[Category: Moulis, J-M.]] | [[Category: Moulis, J-M.]] | ||
[[Category: Sieker, L | [[Category: Sieker, L C.]] | ||
[[Category: Vicat, J.]] | [[Category: Vicat, J.]] | ||
[[Category: SF4]] | [[Category: SF4]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:37:35 2008'' | ||
Revision as of 13:37, 21 February 2008
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REFINED CRYSTAL STRUCTURE OF THE 2[4FE-4S] FERREDOXIN FROM CLOSTRIDIUM ACIDURICI AT 1.84 ANGSTROMS RESOLUTION
OverviewOverview
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.
About this StructureAbout this Structure
1FDN is a Single protein structure of sequence from Clostridium acidurici with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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:7966291
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