Structural highlights
Function
[HYPC_ECOLI] Is required for the formation of all three hydrogenase isoenzymes. May bind to the precursor form of the large subunit of dehydrogenases to keep them in a conformation accessible for metal incorporation.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Solution structure of Escherichia coli HypC.,Wang L, Xia B, Jin C Biochem Biophys Res Commun. 2007 Sep 28;361(3):665-9. Epub 2007 Jul 26. PMID:17669368[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wang L, Xia B, Jin C. Solution structure of Escherichia coli HypC. Biochem Biophys Res Commun. 2007 Sep 28;361(3):665-9. Epub 2007 Jul 26. PMID:17669368 doi:10.1016/j.bbrc.2007.07.094
