1doz

CRYSTAL STRUCTURE OF FERROCHELATASE

spinqualitylabelsall models 1doz, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1doz 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. Ligands: MG Related: 1ak1, 1c1h, 1c9e Activity: Ferrochelatase, with EC number 4.99.1.1 Resources: FirstGlance, OCA, RCSB, PDBsum 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ferrochelatase

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