PMID:17669368

Citation	Wang, L, Xia, B and Jin, C (2007) Solution structure of Escherichia coli HypC. Biochem. Biophys. Res. Commun. 361:665-9
Abstract	Escherichia coli HypC plays an important role in the maturation process of the pre-maturated HycE, the large subunit of hydrogenase 3. It serves as an iron transfer as well as a chaperone protein during the maturation process of pre-HycE, and interacts with both HypD and HycE. The N-terminal cysteine residue of HypC plays a key role in the protein-protein interactions. Here, we present the three-dimensional structure of E. coli HypC, the first solution structure of HupF/HypC family. Our result demonstrates that E. coli HypC consists of a typical OB-fold beta-barrel with two C-terminal helixes. Sequence alignment and structural comparison reveal that the hydrophobic region on the surface of E. coli HypC, as well as the highly flexible C-terminal helixes, may involve in the interactions of E. coli HypC with other proteins.
Links	PubMed Online version:10.1016/j.bbrc.2007.07.094
Keywords	Amino Acid Sequence; Archaeal Proteins/chemistry; Escherichia coli/enzymology; Escherichia coli Proteins/chemistry; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Protein Folding; Protein Structure, Tertiary; Sequence Alignment; Thermococcus/classification; Thermococcus/enzymology
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