2OT2
Solution Structure of HypC
Summary for 2OT2
| Entry DOI | 10.2210/pdb2ot2/pdb |
| NMR Information | BMRB: 15152 |
| Descriptor | Hydrogenase isoenzymes formation protein hypC (1 entity in total) |
| Functional Keywords | beta barrel, chaperone |
| Biological source | Escherichia coli K12 |
| Total number of polymer chains | 1 |
| Total formula weight | 9738.96 |
| Authors | |
| Primary citation | Wang, L.,Xia, B.,Jin, C. Solution structure of Escherichia coli HypC Biochem.Biophys.Res.Commun., 361:665-669, 2007 Cited by PubMed 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. PubMed: 17669368DOI: 10.1016/j.bbrc.2007.07.094 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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