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| {{STRUCTURE_2h1v| PDB=2h1v | SCENE= }} | | {{STRUCTURE_2h1v| PDB=2h1v | SCENE= }} |
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| '''Crystal structure of the Lys87Ala mutant variant of Bacillus subtilis ferrochelatase'''
| | ===Crystal structure of the Lys87Ala mutant variant of Bacillus subtilis ferrochelatase=== |
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| ==Overview==
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| Ferrochelatase catalyzes the terminal step in the heme biosynthetic pathway, i.e., the incorporation of Fe(II) into protoporphyrin IX. Various biochemical and biophysical methods have been used to probe the enzyme for metal binding residues and the location of the active site. However, the location of the metal binding site and the path of the metal into the porphyrin are still disputed. Using site-directed mutagenesis on Bacillus subtilis ferrochelatase we demonstrate that exchange of the conserved residues His183 and Glu264 affects the metal affinity of the enzyme. We also present the first X-ray crystal structure of ferrochelatase with iron. Only a single iron was found in the active site, coordinated in a square pyramidal fashion by two amino acid residues, His183 and Glu264, and three water molecules. This iron was not present in the structure of a His183Ala modified ferrochelatase. The results strongly suggest that the insertion of a metal ion into protoporphyrin IX by ferrochelatase occurs from a metal binding site represented by His183 and Glu264.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17198378}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17198378 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17198378}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Pi-helix]] | | [[Category: Pi-helix]] |
| [[Category: Rossman fold]] | | [[Category: Rossman fold]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:46:28 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:08:34 2008'' |
