1SK7
Structural Basis for Novel Delta-Regioselective Heme Oxygenation in the Opportunistic Pathogen Pseudomonas aeruginosa
Summary for 1SK7
| Entry DOI | 10.2210/pdb1sk7/pdb |
| Descriptor | hypothetical protein pa-HO, SULFATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total) |
| Functional Keywords | heme oxygenase, heme degradation, regioselectivity, oxidoreductase |
| Biological source | Pseudomonas aeruginosa |
| Total number of polymer chains | 1 |
| Total formula weight | 22694.03 |
| Authors | Friedman, J.,Lad, L.,Li, H.,Wilks, A.,Poulos, T.L. (deposition date: 2004-03-04, release date: 2004-06-22, Last modification date: 2023-08-23) |
| Primary citation | Friedman, J.,Lad, L.,Li, H.,Wilks, A.,Poulos, T.L. Structural basis for novel delta-regioselective heme oxygenation in the opportunistic pathogen Pseudomonas aeruginosa Biochemistry, 43:5239-5245, 2004 Cited by PubMed Abstract: The Gram-negative bacterium Pseudomonas aeruginosa contains a heme oxygenase (pa-HO) that primarily oxygenates the delta-meso heme carbon [Caignan, G. A., Deshmukh, R., Wilks, A., Zeng, Y., Huang, H. W., Moenne-Loccoz, P., Bunce, R. A., Eastman, M. A., and Rivera, M. (2002) J. Am. Chem. Soc. 124, 14879-14892]. This differs from other previously characterized heme oxygenases, which display regioselectivity for the alpha-meso heme carbon. Here we report the crystal structure of pa-HO at 1.60 A resolution and compare it to the 1.50 A structure of nm-HO from Neisseria meningitidis [Schuller, D. J., Zhu, W., Stojiljkovic, I., Wilks, A., and Poulos, T. L. (2001) Biochemistry 40, 11552-11558]. The crystal structure of pa-HO maintains the same overall fold as other bacterial and mammalian heme oxygenases, including a conserved network of hydrogen-bonded solvent molecules important for dioxygen activation. The novel delta-regioselectivity of heme oxygenation observed by pa-HO is due to the heme being rotated by approximately 100 degrees, which places the delta-meso heme carbon in the same position as the alpha-meso heme carbon in other heme oxygenases. The main interaction in pa-HO that stabilizes the unique heme orientation is a salt bridge between Lys132 and the heme 7-propionate, as well as hydrophobic contacts involving Leu29, Val33, and Phe189 with the heme methyl and vinyl groups. PubMed: 15122889DOI: 10.1021/bi049687g PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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