|Journal of Molecular Biology (2004) 344(2):567-83|
|Northeast Structural Genomics Consortium|
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IscU is a highly conserved protein that serves as the scaffold for IscS-mediated assembly of iron-sulfur ([Fe-S]) clusters. ...
We report the NMR solution structure of monomeric Haemophilus influenzae IscU with zinc bound at the [Fe-S] cluster assembly site. The compact core of the globular structure has an alpha-beta sandwich architecture with a three-stranded antiparallel beta-sheet and four alpha-helices. A nascent helix is located N-terminal to the core structure. The zinc is ligated by three cysteine residues and one histidine residue that are located in and near conformationally dynamic loops at one end of the IscU structure. Removal of the zinc metal by chelation results in widespread loss of structure in the apo form. The zinc-bound IscU may be a good model for iron-loaded IscU and may demonstrate structural features found in the [Fe-S] cluster bound form. Structural and functional similarities, genomic context in operons containing other homologous genes, and distributions of conserved surface residues support the hypothesis that IscU protein domains are homologous (i.e. derived from a common ancestor) with the SufE/YgdK family of [Fe-S] cluster assembly proteins.
|metabolism chemistry pharmacology |
|Binding Sites Protein Structure, Tertiary Amino Acid Sequence Conserved Sequence Hydrogen Bonding Models, Molecular Molecular Sequence Data Protein Structure, Secondary Histidine Molecular Conformation Sequence Homology, Amino Acid Bacterial Proteins Nuclear Magnetic Resonance, Biomolecular Zinc Evolution, Molecular Ligands Haemophilus influenzae Solutions Iron-Sulfur Proteins Cysteine Spectrum Analysis, Raman Chelating Agents |
|101 (Last update: 03/16/2019 12:23:49pm)|
|multiple pdbids [1q48,1r9p]|