Solution structure of Escherichia coli HypC.
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.
Beijing Nuclear Magnetic Resonance Center, Peking University, Beijing 100871, China.
Lei
L
Wang
Bin
B
Xia
Changwen
C
Jin
D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D019712:Thermococcus / Q000145:classification / Q000201:enzymology
D019843:Archaeal Proteins; D029968:Escherichia coli Proteins; C491587:HypC protein, E coli