1ak1
From Proteopedia
(New page: 200px<br /> <applet load="1ak1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ak1, resolution 1.9Å" /> '''FERROCHELATASE FROM ...) |
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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/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AK1 OCA]]. | + | 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]]. Structure known Active Site: MAL. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AK1 OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9384565 9384565] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9384565 9384565] | ||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
| + | [[Category: Ferrochelatase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Al-Karadaghi, S.]] | [[Category: Al-Karadaghi, S.]] | ||
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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 Oct 30 12:33:30 2007'' |
Revision as of 10:28, 30 October 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, ... [(full description)]
About this Structure
1AK1 is a [Single protein] structure of sequence from [Bacillus subtilis]. Active as [Ferrochelatase], with EC number [4.99.1.1]. Structure known Active Site: MAL. 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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