6fdr: Difference between revisions

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[[Image:6fdr.gif|left|200px]]<br /><applet load="6fdr" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:6fdr.gif|left|200px]]
caption="6fdr, resolution 1.4&Aring;" />
 
'''7-FE FERREDOXIN FROM AZOTOBACTER VINELANDII AT 100K, NA DITHIONITE REDUCED AT PH 8.5, RESOLUTION 1.4 A'''<br />
{{Structure
|PDB= 6fdr |SIZE=350|CAPTION= <scene name='initialview01'>6fdr</scene>, resolution 1.4&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> and <scene name='pdbligand=F3S:FE3-S4 CLUSTER'>F3S</scene>
|ACTIVITY=
|GENE=
}}
 
'''7-FE FERREDOXIN FROM AZOTOBACTER VINELANDII AT 100K, NA DITHIONITE REDUCED AT PH 8.5, RESOLUTION 1.4 A'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
6FDR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with <scene name='pdbligand=SF4:'>SF4</scene> and <scene name='pdbligand=F3S:'>F3S</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1FDC. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FDR OCA].  
6FDR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. This structure supersedes the now removed PDB entry 1FDC. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FDR OCA].  


==Reference==
==Reference==
Oxidized and reduced Azotobacter vinelandii ferredoxin I at 1.4 A resolution: conformational change of surface residues without significant change in the [3Fe-4S]+/0 cluster., Schipke CG, Goodin DB, McRee DE, Stout CD, Biochemistry. 1999 Jun 29;38(26):8228-39. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10387068 10387068]
Oxidized and reduced Azotobacter vinelandii ferredoxin I at 1.4 A resolution: conformational change of surface residues without significant change in the [3Fe-4S]+/0 cluster., Schipke CG, Goodin DB, McRee DE, Stout CD, Biochemistry. 1999 Jun 29;38(26):8228-39. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10387068 10387068]
[[Category: Azotobacter vinelandii]]
[[Category: Azotobacter vinelandii]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: iron-sulfur]]
[[Category: iron-sulfur]]


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Revision as of 20:13, 20 March 2008

File:6fdr.gif


PDB ID 6fdr

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, resolution 1.4Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



7-FE FERREDOXIN FROM AZOTOBACTER VINELANDII AT 100K, NA DITHIONITE REDUCED AT PH 8.5, RESOLUTION 1.4 A


OverviewOverview

The refined structure of reduced Azotobacter vinelandii 7Fe ferredoxin FdI at 100 K and 1.4 A resolution is reported, permitting comparison of [3Fe-4S]+ and [3Fe-4S]0 clusters in the same protein at near atomic resolution. The reduced state of the [3Fe-4S]0 cluster is established by single-crystal EPR following data collection. Redundant structures are refined to establish the reproducibility and accuracy of the results for both oxidation states. The structure of the [4Fe-4S]2+ cluster in four independently determined FdI structures is the same within the range of derived standard uncertainties, providing an internal control on the experimental methods and the refinement results. The structures of the [3Fe-4S]+ and [3Fe-4S]0 clusters are also the same within experimental error, indicating that the protein may be enforcing an entatic state upon this cluster, facilitating electron-transfer reactions. The structure of the FdI [3Fe-4S]0 cluster allows direct comparison with the structure of a well-characterized [Fe3S4]0 synthetic analogue compound. The [3Fe-4S]0 cluster displays significant distortions with respect to the [Fe3S4]0 analogue, further suggesting that the observed [3Fe-4S]+/0 geometry in FdI may represent an entatic state. Comparison of oxidized and reduced FdI reveals conformational changes at the protein surface in response to reduction of the [3Fe-4S]+/0 cluster. The carboxyl group of Asp15 rotates approximately 90 degrees, Lys84, a residue hydrogen bonded to Asp15, adopts a single conformation, and additional H2O molecules become ordered. These structural changes imply a mechanism for H+ transfer to the [3Fe-4S]0 cluster in agreement with electrochemical and spectroscopic results.

About this StructureAbout this Structure

6FDR is a Single protein structure of sequence from Azotobacter vinelandii. This structure supersedes the now removed PDB entry 1FDC. Full crystallographic information is available from OCA.

ReferenceReference

Oxidized and reduced Azotobacter vinelandii ferredoxin I at 1.4 A resolution: conformational change of surface residues without significant change in the [3Fe-4S]+/0 cluster., Schipke CG, Goodin DB, McRee DE, Stout CD, Biochemistry. 1999 Jun 29;38(26):8228-39. PMID:10387068

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