2I8L
Solution Structure of an endopeptidase HycI from Escherichia coli
Summary for 2I8L
| Entry DOI | 10.2210/pdb2i8l/pdb |
| Descriptor | Hydrogenase 3 maturation protease (1 entity in total) |
| Functional Keywords | alpha-beta sandwich, hydrolase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 17066.43 |
| Authors | |
| Primary citation | Yang, F.,Hu, W.,Xu, H.,Li, C.,Xia, B.,Jin, C. Solution structure and backbone dynamics of an endopeptidase HycI from Escherichia coli: implications for mechanism of the [NiFe] hydrogenase maturation J.Biol.Chem., 282:3856-3863, 2007 Cited by PubMed Abstract: [NiFe] hydrogenases are metalloenzymes involved in many biological processes concerning the metabolism of hydrogen. The maturation of the large subunit of these hydrogenases requires the cleavage of a peptide at the C terminus by an endopeptidase before the final formation of the [NiFe] metallocenter. HycI is an endopeptidase of the M52 family and responsible for the C-terminal cleavage of the large subunit of hydrogenase 3 in Escherichia coli. Although extensive studies were performed, the molecular mechanism of recognition and cleavage of hydrogenase 3 remains elusive. Herein, we report the solution structure of E. coli HycI determined by high resolution nuclear magnetic resonance spectroscopy. This is the first solution structure of the apo form of endopeptidase of the M52 family reported thus far. The overall structure is similar to the crystal structure of holo-HybD in the same family. However, significant diversity was observed between the two structures. Especially, HycI shows an open conformation at the putative nickel-binding site, whereas HybD adopts a closed conformation. In addition, we performed backbone dynamic studies to probe the motional properties of the apo form of HycI. Furthermore, the metal ion titration experiments provide insightful information on the substrate recognition and cleavage processes. Taken together, our current structural, biochemical, and dynamic studies extend the knowledge of the M52 family proteins and provide novel insights into the biological function of HycI. PubMed: 17150961DOI: 10.1074/jbc.M609263200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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