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Updated: Jul 13, 2026

A Toolkit to Enable Hydrocarbon Conversion in Aqueous Environments

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Published on: October 2, 2012

Solution structure of Escherichia coli HypC.

Lei Wang¹, Bin Xia, Changwen Jin

¹Beijing Nuclear Magnetic Resonance Center, Peking University, Beijing 100871, China.

Biochemical and Biophysical Research Communications

|August 3, 2007

Summary

Escherichia coli HypC protein is crucial for hydrogenase 3 maturation. Its 3D structure reveals an OB-fold beta-barrel, explaining its role in protein interactions during maturation.

Area of Science:

Biochemistry
Structural Biology
Microbiology

Background:

Escherichia coli HypC protein is essential for the maturation of hydrogenase 3, specifically the HycE subunit.
HypC functions as an iron transfer and chaperone protein, interacting with HypD and HycE during pre-HycE maturation.
The N-terminal cysteine residue of HypC is critical for its protein-protein interactions.

Purpose of the Study:

To determine the three-dimensional structure of Escherichia coli HypC.
To elucidate the structural basis for HypC's role in hydrogenase maturation and protein interactions.

Main Methods:

Nuclear Magnetic Resonance (NMR) spectroscopy was used to determine the solution structure of E. coli HypC.
Sequence alignment and structural comparison with related proteins were performed.

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Main Results:

The first solution structure of a HupF/HypC family protein, E. coli HypC, was determined.
E. coli HypC exhibits a characteristic OB-fold beta-barrel structure with two C-terminal helices.
A surface hydrophobic region and flexible C-terminal helices were identified as potential interaction sites for other proteins.

Conclusions:

The determined 3D structure of E. coli HypC provides insights into its function in hydrogenase maturation.
Structural features like the hydrophobic surface and flexible helices likely mediate interactions with HypD and HycE.
This study presents the first structural data for the HupF/HypC family, opening avenues for further research.