7fdr: Difference between revisions

Revision as of 22:44, 4 May 2008

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

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

7FDR is a Single protein structure of sequence from Azotobacter vinelandii. 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 Page seeded by OCA on Sun May 4 22:44:50 2008

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OCA

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 [[Image:7fdr.gif|left|200px]]
- {{Structure
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-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=7fdr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fdr OCA], [http://www.ebi.ac.uk/pdbsum/7fdr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=7fdr RCSB]</span>
-}}
 '''7-FE FERREDOXIN FROM AZOTOBACTER VINELANDII, NA DITHIONITE REDUCED, PH 8.5, 1.4A RESOLUTION, 100 K'''
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 [[Category: Schipke, C G.]]
 [[Category: Stout, C D.]]
-[[Category: electron transport]]
+[[Category: Electron transport]]
-[[Category: iron-sulfur]]
+[[Category: Iron-sulfur]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:44:50 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:44:01 2008''