1ff2
From Proteopedia
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|PDB= 1ff2 |SIZE=350|CAPTION= <scene name='initialview01'>1ff2</scene>, resolution 2.30Å | |PDB= 1ff2 |SIZE=350|CAPTION= <scene name='initialview01'>1ff2</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[6fd1|6FD1]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ff2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ff2 OCA], [http://www.ebi.ac.uk/pdbsum/1ff2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ff2 RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Burgess, B K.]] | [[Category: Burgess, B K.]] | ||
[[Category: Stout, C D.]] | [[Category: Stout, C D.]] | ||
| - | [[Category: F3S]] | ||
| - | [[Category: SF4]] | ||
[[Category: 7fe ferredoxin]] | [[Category: 7fe ferredoxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:21:37 2008'' |
Revision as of 17:21, 30 March 2008
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| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 6FD1
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE C42D MUTANT OF AZOTOBACTER VINELANDII 7FE FERREDOXIN (FDI)
Overview
All naturally occurring ferredoxins that have Cys-X-X-Asp-X-X-Cys motifs contain [4Fe-4S](2+/+) clusters that can be easily and reversibly converted to [3Fe-4S](+/0) clusters. In contrast, ferredoxins with unmodified Cys-X-X-Cys-X-X-Cys motifs assemble [4Fe-4S](2+/+) clusters that cannot be easily interconverted with [3Fe-4S](+/0) clusters. In this study we changed the central cysteine of the Cys(39)-X-X-Cys(42)-X-X-Cys(45) of Azotobacter vinelandii FdI, which coordinates its [4Fe-4S](2+/+) cluster, into an aspartate. UV-visible, EPR, and CD spectroscopies, metal analysis, and x-ray crystallography show that, like native FdI, aerobically purified C42D FdI is a seven-iron protein retaining its [4Fe-4S](2+/+) cluster with monodentate aspartate ligation to one iron. Unlike known clusters of this type the reduced [4Fe-4S](+) cluster of C42D FdI exhibits only an S = 1/2 EPR with no higher spin signals detected. The cluster shows only a minor change in reduction potential relative to the native protein. All attempts to convert the cluster to a 3Fe cluster using conventional methods of oxygen or ferricyanide oxidation or thiol exchange were not successful. The cluster conversion was ultimately accomplished using a new electrochemical method. Hydrophobic and electrostatic interaction and the lack of Gly residues adjacent to the Asp ligand explain the remarkable stability of this cluster.
About this Structure
1FF2 is a Single protein structure of sequence from Azotobacter vinelandii. Full crystallographic information is available from OCA.
Reference
Structure of C42D Azotobacter vinelandii FdI. A Cys-X-X-Asp-X-X-Cys motif ligates an air-stable [4Fe-4S]2+/+ cluster., Jung YS, Bonagura CA, Tilley GJ, Gao-Sheridan HS, Armstrong FA, Stout CD, Burgess BK, J Biol Chem. 2000 Nov 24;275(47):36974-83. PMID:10961993
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