PMID:15153099
| Citation |
Adinolfi, S, Rizzo, F, Masino, L, Nair, M, Martin, SR, Pastore, A and Temussi, PA (2004) Bacterial IscU is a well folded and functional single domain protein. Eur. J. Biochem. 271:2093-100 |
|---|---|
| Abstract |
Iron-sulfur clusters are widely represented in most organisms, but the mechanism of their formation is not fully understood. Of the two main proteins involved in cluster formation, NifS/IscS and NifU/IscU, only the former has been well studied from a structural point of view. Here we report an extensive structural characterization of Escherichia coli IscU. We show by a variety of physico-chemical techniques that E. coli IscU construct can be expressed to high purity as a monomeric protein, characterized by an alphabeta fold with high alpha-helix content. The high melting temperature and the reversibility of the thermal unfolding curve (as measured by CD spectroscopy) hint at a well ordered stable fold. The excellent dispersion of cross peaks in the (1)H-(15)N correlation spectrum is consistent with these observations. Monomeric E. coli IscU is able to provide a scaffold for Iron-sulfur cluster assembly, but has no direct interaction with either Fe(II) or Fe(III) ions, suggesting the need of further partners to achieve a stable interaction. |
| Links |
PubMed Online version:10.1111/j.1432-1033.2004.04112.x |
| Keywords |
Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Iron/chemistry; Iron/metabolism; Iron-Sulfur Proteins/chemistry; Iron-Sulfur Proteins/genetics; Iron-Sulfur Proteins/metabolism; Nuclear Magnetic Resonance, Biomolecular; Protein Binding; Protein Denaturation; Protein Folding; Protein Structure, Tertiary; Recombinant Proteins/chemistry; Sulfur/chemistry; Temperature |
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