4KIA
Crystal structure of LmHde, heme-degrading enzyme, from Listeria monocytogenes
Summary for 4KIA
| Entry DOI | 10.2210/pdb4kia/pdb |
| Descriptor | Lmo2213 protein (2 entities in total) |
| Functional Keywords | ferredoxin fold, heme-degrading enzyme, heme binding, oxidoreductase |
| Biological source | Listeria monocytogenes |
| Total number of polymer chains | 1 |
| Total formula weight | 19771.44 |
| Authors | |
| Primary citation | Duong, T.,Park, K.,Kim, T.,Kang, S.W.,Hahn, M.J.,Hahn, M.J.,Hwang, H.Y.,Jang, I.,Oh, H.B.,Kim, K.K. Structural and functional characterization of an Isd-type haem-degradation enzyme from Listeria monocytogenes. Acta Crystallogr.,Sect.D, 70:615-626, 2014 Cited by PubMed Abstract: Bacterial pathogens have evolved diverse types of efficient machinery to acquire haem, the most abundant source of iron in the human body, and degrade it for the utilization of iron. Gram-positive bacteria commonly encode IsdG-family proteins as haem-degrading monooxygenases. Listeria monocytogenes is predicted to possess an IsdG-type protein (Lmo2213), but the residues involved in haem monooxygenase activity are not well conserved and there is an extra N-terminal domain in Lmo2213. Therefore, its function and mechanism of action cannot be predicted. In this study, the crystal structure of Lmo2213 was determined at 1.75 Å resolution and its haem-binding and haem-degradation activities were confirmed. Structure-based mutational and functional assays of this protein, designated as an Isd-type L. monocytogenes haem-degrading enzyme (Isd-LmHde), identified that Glu71, Tyr87 and Trp129 play important roles in haem degradation and that the N-terminal domain is also critical for its haem-degrading activity. The haem-degradation product of Isd-LmHde is verified to be biliverdin, which is also known to be the degradation product of other bacterial haem oxygenases. This study, the first structural and functional report of the haem-degradation system in L. monocytogenes, sheds light on the concealed haem-utilization system in this life-threatening human pathogen. PubMed: 24598731DOI: 10.1107/S1399004713030794 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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