DOI QR코드

DOI QR Code

Bacillus subtilis HmoB is a heme oxygenase with a novel structure

  • Park, Seong-Hun (Department of Life Science, University of Seoul) ;
  • Choi, Sa-Rah (Department of Life Science, University of Seoul) ;
  • Choe, Jung-Woo (Department of Life Science, University of Seoul)
  • Received : 2011.10.05
  • Accepted : 2011.12.23
  • Published : 2012.04.30

Abstract

Iron availability is limited in the environment and most bacteria have developed a system to acquire iron from host hemoproteins. Heme oxygenase plays an important role by degrading heme group and releasing the essential nutrient iron. The structure of Bacillus subtilis HmoB was determined to 2.0 ${\AA}$ resolution. B. subtilis HmoB contains a typical antibiotic biosynthesis monooxygenase (ABM) domain that spans from 71 to 146 residues and belongs to the IsdG family heme oxygenases. Comparison of HmoB and IsdG family proteins showed that the C-terminal region of HmoB has similar sequence and structure to IsdG family proteins and contains conserved critical residues for heme degradation. However, HmoB is distinct from other IsdG family proteins in that HmoB is about 60 amino acids longer in the N-terminus and does not form a dimer whereas previously studied IsdG family heme oxygenases form functional homodimers. Interestingly, the structure of monomeric HmoB resembles the dimeric structure of IsdG family proteins. Hence, B. subtilis HmoB is a heme oxygenase with a novel structural feature.

Keywords

Antibiotic biosynthesis domain;Crystallography;Ferredoxin-fold;Heme oxygenase

Acknowledgement

Supported by : National Research Foundation of Korea (NRF)

References

  1. Wandersman, C. and Delepelaire, P. (2004) Bacterial iron sources: from siderophores to hemophores. Annu. Rev. Microbiol. 58, 611-647. https://doi.org/10.1146/annurev.micro.58.030603.123811
  2. Ratledge, C. and Dover, L. G. (2000) Iron metabolism in pathogenic bacteria. Annu. Rev. Microbiol 54, 881-941. https://doi.org/10.1146/annurev.micro.54.1.881
  3. Skaar, E. P. and Schneewind, O. (2004) Iron-regulated surface determinants (Isd) of Staphylococcus aureus: stealing iron from heme. Microbes. Infect. 6, 390-397. https://doi.org/10.1016/j.micinf.2003.12.008
  4. Skaar, E. P., Gaspar, A. H. and Schneewind, O. (2004) IsdG and IsdI, heme-degrading enzymes in the cytoplasm of Staphylococcus aureus. J. Biol. Chem. 279, 436-443. https://doi.org/10.1074/jbc.M307952200
  5. Gaballa, A. and Helmann, J. D. (2011) Bacillus subtilis Fur represses one of two paralogous haem-degrading monooxygenases. Microbiology 157, 3221-3231. https://doi.org/10.1099/mic.0.053579-0
  6. Orengo, C. A. and Thornton, J. M. (1993) Alpha plus beta folds revisited: some favoured motifs. Structure 1, 105-120. https://doi.org/10.1016/0969-2126(93)90026-D
  7. Reynolds, C., Damerell, D. and Jones, S. (2009) ProtorP: a protein-protein interaction analysis server. Bioinformatics 25, 413-414. https://doi.org/10.1093/bioinformatics/btn584
  8. Jones, S. and Thornton, J. M. (1997) Analysis of protein-protein interaction sites using surface patches. J. Mol. Biol. 272, 121-132. https://doi.org/10.1006/jmbi.1997.1234
  9. Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326. https://doi.org/10.1016/S0076-6879(97)76066-X
  10. Adams, P. D., Afonine, P. V., Bunkoczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L. W., Kapral, G. J., Grosse-Kunstleve, R. W., McCoy, A. J., Moriarty, N. W., Oeffner, R., Read, R. J., Richardson, D. C., Richardson, J. S., Terwilliger, T. C. and Zwart, P. H. (2010) PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta. Crystallogr. D. Biol. Crystallogr. 66, 213-221. https://doi.org/10.1107/S0907444909052925
  11. Murshudov, G. N., Vagin, A. A. and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta. Crystallogr. D. Biol. Crystallogr. 53, 240-255. https://doi.org/10.1107/S0907444996012255
  12. Emsley, P., Lohkamp, B., Scott, W. G. and Cowtan, K. (2010) Features and development of Coot. Acta. Crystallogr. D. Biol. Crystallogr 66, 486-501. https://doi.org/10.1107/S0907444910007493
  13. Laskowski, R. A., Rullmannn, J. A., MacArthur, M. W., Kaptein, R. and Thornton, J. M. (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8, 477-486.

Cited by

  1. Structural and functional characterization of an Isd-type haem-degradation enzyme fromListeria monocytogenes vol.70, pp.3, 2014, https://doi.org/10.1107/S1399004713030794
  2. Structural and biochemical study of Bacillus subtilis HmoB in complex with heme vol.446, pp.1, 2014, https://doi.org/10.1016/j.bbrc.2014.02.092
  3. Recent developments in understanding the iron acquisition strategies of gram positive pathogens vol.39, pp.4, 2015, https://doi.org/10.1093/femsre/fuv009