|Journal of Molecular Biology (2004) 344(2):567-83|
|Northeast Structural Genomics Consortium|
(click to unfold)
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 |
|Haemophilus influenzae Protein Structure, Tertiary Conserved Sequence Iron-Sulfur Proteins Spectrum Analysis, Raman Ligands Binding Sites Protein Structure, Secondary Amino Acid Sequence Nuclear Magnetic Resonance, Biomolecular Sequence Homology, Amino Acid Bacterial Proteins Histidine Hydrogen Bonding Models, Molecular Molecular Sequence Data Evolution, Molecular Cysteine Zinc Chelating Agents Solutions Molecular Conformation |
|89 (Last update: 04/01/2017 11:38:44am)|
|multiple pdbids [1q48,1r9p]|