3O72
Crystal structure of EfeB in complex with heme
Summary for 3O72
| Entry DOI | 10.2210/pdb3o72/pdb |
| Descriptor | Redox component of a tripartite ferrous iron transporter, PROTOPORPHYRIN IX CONTAINING FE, OXYGEN MOLECULE, ... (4 entities in total) |
| Functional Keywords | efeb in complex with heme, heme deferrochelatase, heme binding, heme-binding protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 4 |
| Total formula weight | 180241.77 |
| Authors | |
| Primary citation | Liu, X.,Du, Q.,Wang, Z.,Zhu, D.,Huang, Y.,Li, N.,Wei, T.,Xu, S.,Gu, L. Crystal structure and biochemical features of EfeB/YcdB from Escherichia coli O157: ASP235 plays divergent roles in different enzyme-catalyzed processes J.Biol.Chem., 286:14922-14931, 2011 Cited by PubMed Abstract: EfeB/YcdB is a member of the dye-decolorizing peroxidase (DyP) protein family. A recent study has shown that this protein can extract iron from heme without breaking the tetrapyrrole ring. We report the crystal structure of EfeB from Escherichia coli O157 bound to heme at 1.95 Å resolution. The EfeB monomer contains two domains. The heme molecule is located in a large hydrophobic pocket in the C-terminal domain. A long loop connecting the two domains extensively interacts with the heme, which is a distinctive structural feature of EfeB homologues. A large tunnel formed by this loop and the β-sheet of C-terminal domain provides a potential cofactor/substrate binding site. Biochemical data show that the production of protoporphyrin IX (PPIX) is closely related to the peroxidation activity. The mutant D235N keeps nearly the same activity of guaiacol peroxidase as the wild-type protein, whereas the corresponding mutation in the classic DyP protein family completely abolished the peroxidation activity. These results suggest that EfeB is a unique member of the DyP protein family. In addition, dramatically enhanced fluorescence excitation and emission of EfeB-PPIX was observed, implying this protein may be used as a red color fluorescence marker. PubMed: 21324904DOI: 10.1074/jbc.M110.197780 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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