1frx
From Proteopedia
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STRUCTURE AND PROPERTIES OF C20S FDI MUTANT
Overview
The [4Fe-4S] cluster of Azotobacter vinelandii ferredoxin I receives three, of its four ligands from a Cys-Xaa-Xaa-Cys-Xaa-Xaa-Cys sequence at, positions 39-45 while the fourth ligand, Cys20, is provided by a distal, portion of the sequence. Previously we reported that the site-directed, mutation of Cys20 to Ala (C20A protein) resulted in the formation of a new, [4Fe-4S] cluster that obtained its fourth ligand from Cys24, a free, cysteine in the native structure. That ligand exchange required, significant protein rearrangement. Here we report the conversion of Cys20, to Ser (C20S protein), which gives the protein the opportunity either to, retain the native structure and use the Ser20 O gamma as a ligand or to, rearrange and use Cys24. X-ray crystallography demonstrates that the, cluster does not use the Ser20 O gamma as a ligand; rather it rearranges, to use Cys24. In the C20S protein the [4Fe-4S] cluster has altered, stability and redox properties relative to either C20A or the native, protein.
About this Structure
1FRX is a Single protein structure of sequence from Azotobacter vinelandii with SF4 and F3S as ligands. Full crystallographic information is available from OCA.
Reference
Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: cysteine ligation of the [4Fe-4S] cluster with protein rearrangement is preferred over serine ligation., Shen B, Jollie DR, Diller TC, Stout CD, Stephens PJ, Burgess BK, Proc Natl Acad Sci U S A. 1995 Oct 24;92(22):10064-8. PMID:7479727
Page seeded by OCA on Tue Nov 20 15:12:50 2007
