1c9e
From Proteopedia
(New page: 200px<br /><applet load="1c9e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c9e, resolution 2.30Å" /> '''STRUCTURE OF FERROCH...) |
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| - | [[Image:1c9e.gif|left|200px]]<br /><applet load="1c9e" size=" | + | [[Image:1c9e.gif|left|200px]]<br /><applet load="1c9e" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1c9e, resolution 2.30Å" /> | caption="1c9e, resolution 2.30Å" /> | ||
'''STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE'''<br /> | '''STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Ferrochelatase, the enzyme catalyzing metallation of protoporphyrin IX at | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1C9E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with MG and MP1 as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Full crystallographic information is available from [http:// | + | 1C9E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=MP1:'>MP1</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C9E OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Al-Karadaghi, S.]] | [[Category: Al-Karadaghi, S.]] | ||
| - | [[Category: Fodje, M | + | [[Category: Fodje, M N.]] |
[[Category: Hansson, A.]] | [[Category: Hansson, A.]] | ||
[[Category: Hansson, M.]] | [[Category: Hansson, M.]] | ||
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[[Category: porphyrin metallation]] | [[Category: porphyrin metallation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:03:47 2008'' |
Revision as of 10:03, 21 February 2008
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STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE
Overview
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.
About this Structure
1C9E is a Single protein structure of sequence from Bacillus subtilis with and as ligands. Active as Ferrochelatase, with EC number 4.99.1.1 Full crystallographic information is available from OCA.
Reference
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
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