2hk6

Crystal Structure of B. subtilis ferrochelatase with Iron bound at the active siteCrystal Structure of B. subtilis ferrochelatase with Iron bound at the active site

Structural highlights 2hk6 is a 1 chain structure with sequence from "bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , Related: 1doz Gene: hemH, hemF ("Bacillus globigii" Migula 1900) Activity: Ferrochelatase, with EC number 4.99.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [HEMH_BACSU] Catalyzes the ferrous insertion into protoporphyrin IX. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Amino acid residues His183 and Glu264 in Bacillus subtilis ferrochelatase direct and facilitate the insertion of metal ion into protoporphyrin IX.,Hansson MD, Karlberg T, Rahardja MA, Al-Karadaghi S, Hansson M Biochemistry. 2007 Jan 9;46(1):87-94. PMID:17198378 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ferrochelatase

spinqualitylabelsall models 2hk6, resolution 1.71Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image