1c9e is a 1 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
CPFC_BACSU Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:25646457, PubMed:25908396). Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III (PubMed:25646457, PubMed:25908396). It can also insert iron into protoporphyrin IX (PubMed:1459957, PubMed:21052751, PubMed:25646457, PubMed:8119288). Has weaker activity with 2,4 disulfonate, deuteroporphyrin and 2,4 hydroxyethyl (PubMed:12761666, PubMed:25646457). In vitro, can also use Zn(2+) or Cu(2+) (PubMed:12761666, PubMed:16140324, PubMed:21052751, PubMed:8119288).[1][2][3][4][5][6][7][8]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structural and mechanistic basis of porphyrin metallation by ferrochelatase.,Lecerof D, Fodje M, Hansson A, Hansson M, Al-Karadaghi S J Mol Biol. 2000 Mar 17;297(1):221-32. PMID:10704318[9]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑Lecerof D, Fodje MN, Alvarez Leon R, Olsson U, Hansson A, Sigfridsson E, Ryde U, Hansson M, Al-Karadaghi S. Metal binding to Bacillus subtilis ferrochelatase and interaction between metal sites. J Biol Inorg Chem. 2003 Apr;8(4):452-8. Epub 2003 Jan 18. PMID:12761666 doi:10.1007/s00775-002-0436-1
↑Hansson M, Hederstedt L. Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes. J Bacteriol. 1992 Dec;174(24):8081-93. PMID:1459957 doi:10.1128/jb.174.24.8081-8093.1992
↑Shipovskov S, Karlberg T, Fodje M, Hansson MD, Ferreira GC, Hansson M, Reimann CT, Al-Karadaghi S. Metallation of the transition-state inhibitor N-methyl mesoporphyrin by ferrochelatase: implications for the catalytic reaction mechanism. J Mol Biol. 2005 Oct 7;352(5):1081-90. PMID:16140324 doi:10.1016/j.jmb.2005.08.002
↑Hansson MD, Karlberg T, Soderberg CA, Rajan S, Warren MJ, Al-Karadaghi S, Rigby SE, Hansson M. Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of Bacillus subtilis ferrochelatase. J Biol Inorg Chem. 2010 Nov 4. PMID:21052751 doi:10.1007/s00775-010-0720-4
↑Dailey HA, Gerdes S, Dailey TA, Burch JS, Phillips JD. Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin. Proc Natl Acad Sci U S A. 2015 Feb 17;112(7):2210-5. PMID:25646457 doi:10.1073/pnas.1416285112
↑Mielcarek A, Blauenburg B, Miethke M, Marahiel MA. Molecular insights into frataxin-mediated iron supply for heme biosynthesis in Bacillus subtilis. PLoS One. 2015 Mar 31;10(3):e0122538. PMID:25826316 doi:10.1371/journal.pone.0122538
↑Lobo SA, Scott A, Videira MA, Winpenny D, Gardner M, Palmer MJ, Schroeder S, Lawrence AD, Parkinson T, Warren MJ, Saraiva LM. Staphylococcus aureus haem biosynthesis: characterisation of the enzymes involved in final steps of the pathway. Mol Microbiol. 2015 Aug;97(3):472-87. PMID:25908396 doi:10.1111/mmi.13041
↑Hansson M, Hederstedt L. Purification and characterisation of a water-soluble ferrochelatase from Bacillus subtilis. Eur J Biochem. 1994 Feb 15;220(1):201-8. PMID:8119288 doi:10.1111/j.1432-1033.1994.tb18615.x
↑Lecerof D, Fodje M, Hansson A, Hansson M, Al-Karadaghi S. Structural and mechanistic basis of porphyrin metallation by ferrochelatase. J Mol Biol. 2000 Mar 17;297(1):221-32. PMID:10704318 doi:10.1006/jmbi.2000.3569
