1ak1
From Proteopedia
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| - | [[Image:1ak1.gif|left|200px]]<br /> | + | [[Image:1ak1.gif|left|200px]]<br /><applet load="1ak1" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ak1" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1ak1, resolution 1.9Å" /> | caption="1ak1, resolution 1.9Å" /> | ||
'''FERROCHELATASE FROM BACILLUS SUBTILIS'''<br /> | '''FERROCHELATASE FROM BACILLUS SUBTILIS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AK1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Active as [http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] | + | 1AK1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Active as [http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] Known structural/functional Site: <scene name='pdbsite=MAL:In The Au And Cd Derivatives The Metal Ions Were Bound T ...'>MAL</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AK1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protoheme ferro-lyase]] | [[Category: protoheme ferro-lyase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:16:22 2007'' |
Revision as of 12:06, 18 December 2007
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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, replacement. The structural model contains 308 of the 310 amino acid, residues of the protein and 198 solvent molecules. The polypeptide is, folded into two similar domains each with a four-stranded parallel beta, sheet flanked by alpha helices. Structural elements from both domains, build up a cleft, which contains several amino acid residues that are, invariant in ferrochelatases from different organisms. In crystals soaked, with gold and cadmium salt solutions, the metal ion was found to be, coordinated to the conserved residue His 183, which is located in the, cleft. This histidine residue has previously been suggested to be involved, in ferrous ion binding. CONCLUSIONS: Ferrochelatase seems to have a, structurally conserved core region that is common to the enzyme from, bacteria, plants and mammals. We propose that porphyrin binds in the, identified cleft; this cleft also includes the metal-binding site of the, enzyme. It is likely that the structure of the cleft region will have, different conformations upon substrate binding and release.
About this Structure
1AK1 is a Single protein structure of sequence from Bacillus subtilis. Active as Ferrochelatase, with EC number 4.99.1.1 Known structural/functional Site: . 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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