1c1h
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(New page: 200px<br /><applet load="1c1h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c1h, resolution 1.90Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 09:57, 20 November 2007
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CRYSTAL STRUCTURE OF BACILLUS SUBTILIS FERROCHELATASE IN COMPLEX WITH N-METHYL MESOPORPHYRIN
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
1C1H is a Single protein structure of sequence from Bacillus subtilis with MG and MMP 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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