1C9E
STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE
Summary for 1C9E
| Entry DOI | 10.2210/pdb1c9e/pdb |
| Related | 1ak1 1c1h |
| Descriptor | PROTOHEME FERROLYASE, MAGNESIUM ION, N-METHYLMESOPORPHYRIN CONTAINING COPPER, ... (4 entities in total) |
| Functional Keywords | bacillus subtilis, chelatase, porphyrin metallation, n-methylmesoporphyrin, heme synthesis, lyase |
| Biological source | Bacillus subtilis |
| Cellular location | Cytoplasm: P32396 |
| Total number of polymer chains | 1 |
| Total formula weight | 35552.62 |
| Authors | Lecerof, D.,Fodje, M.N.,Hansson, A.,Hansson, M.,Al-Karadaghi, S. (deposition date: 1999-08-02, release date: 2000-03-22, Last modification date: 2024-02-07) |
| Primary citation | Lecerof, D.,Fodje, M.,Hansson, A.,Hansson, M.,Al-Karadaghi, S. Structural and mechanistic basis of porphyrin metallation by ferrochelatase. J.Mol.Biol., 297:221-232, 2000 Cited by PubMed Abstract: Ferrochelatase, the enzyme catalyzing metallation of protoporphyrin IX at the terminal step of heme biosynthesis, was co-crystallized with an isomer mixture of the potent inhibitor N-methylmesoporphyrin (N-MeMP). The X-ray structure revealed the active site of the enzyme, to which only one of the isomers was bound, and for the first time allowed characterization of the mode of porphyrin macrocycle distortion by ferrochelatase. Crystallization of ferrochelatase and N-MeMP in the presence of Cu(2+) leads to metallation and demethylation of N-MeMP. A mechanism of porphyrin distortion is proposed, which assumes that the enzyme holds pyrrole rings B, C and D in a vice-like grip and forces a 36 degrees tilt on ring A. PubMed: 10704318DOI: 10.1006/jmbi.2000.3569 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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