1FD2

SITE-DIRECTED MUTAGENESIS OF AZOTOBACTER VINELANDII FERREDOXIN I. (FE-S) CLUSTER-DRIVEN PROTEIN REARRANGEMENT

Summary for 1FD2

• Entry DOI: 10.2210/pdb1fd2/pdb
• Related: 2FD2 4FD1
• Descriptor: FERREDOXIN, IRON/SULFUR CLUSTER, FE3-S4 CLUSTER, ... (4 entities in total)
• Functional Keywords: electron transfer(iron-sulfur protein)
• Biological source: Azotobacter vinelandii
• Total number of polymer chains: 1
• Total formula weight: 12674.90

Authors

Stout, C.D. (deposition date: 1988-12-08, release date: 1989-10-15, Last modification date: 2024-02-07)

Primary citation

Martin, A.E.,Burgess, B.K.,Stout, C.D.,Cash, V.L.,Dean, D.R.,Jensen, G.M.,Stephens, P.J.
Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: [Fe-S] cluster-driven protein rearrangement.
Proc.Natl.Acad.Sci.USA, 87:598-602, 1990

PubMed Abstract: Azotobacter vinelandii ferredoxin I is a small protein that contains one [4Fe-4S] cluster and one [3Fe-4S] cluster. Recently the x-ray crystal structure has been redetermined and the fdxA gene, which encodes the protein, has been cloned and sequenced. Here we report the site-directed mutation of Cys-20, which is a ligand of the [4Fe-4S] cluster in the native protein, to alanine and the characterization of the protein product by x-ray crystallographic and spectroscopic methods. The data show that the mutant protein again contains one [4Fe-4S] cluster and one [3Fe-4S] cluster. The new [4Fe-4S] cluster obtains its fourth ligand from Cys-24, a free cysteine in the native structure. The formation of this [4Fe-4S] cluster drives rearrangement of the protein structure.

PubMed: 2153958
DOI: 10.1073/pnas.87.2.598

Experimental method

X-RAY DIFFRACTION (1.9 Å)