1ak1
From Proteopedia
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FERROCHELATASE FROM BACILLUS SUBTILIS
Overview
BACKGROUND: The metallation of closed ring tetrapyrroles resulting in the, formation of hemes, chlorophylls and vitamin B12 is catalyzed by specific, enzymes called chelatases. Ferrochelatase catalyzes the terminal step in, heme biosynthesis by inserting ferrous ion into protoporphyrin IX by a, mechanism that is poorly understood. Mutations in the human gene for, ferrochelatase can result in the disease erythropoietic protoporphyria, and a further understanding of the mechanism of this enzyme is therefore, of clinical interest. No three-dimensional structure of a tetrapyrrole, metallation enzyme has been available until now. Results: The, three-dimensional structure of Bacillus subtilis ferrochelatase has been, determined at 1.9 A resolution by the method of multiple isomorphous, ... [(full description)]
About this Structure
1AK1 is a [Single protein] structure of sequence from [Bacillus subtilis]. Active as [[1]], with EC number [4.99.1.1]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis., Al-Karadaghi S, Hansson M, Nikonov S, Jonsson B, Hederstedt L, Structure. 1997 Nov 15;5(11):1501-10. PMID:9384565
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