1c9e

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{{STRUCTURE_1c9e| PDB=1c9e | SCENE= }}
{{STRUCTURE_1c9e| PDB=1c9e | SCENE= }}
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'''STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE'''
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===STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10704318 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10704318}}
==About this Structure==
==About this Structure==
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[[Category: N-methylmesoporphyrin]]
[[Category: N-methylmesoporphyrin]]
[[Category: Porphyrin metallation]]
[[Category: Porphyrin metallation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:29:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:24:09 2008''

Revision as of 17:24, 30 June 2008

Image:1c9e.png

Template:STRUCTURE 1c9e

STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE

Template:ABSTRACT PUBMED 10704318

About this Structure

1C9E is a Single protein structure of sequence from Bacillus subtilis. 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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