2H1V

Crystal structure of the Lys87Ala mutant variant of Bacillus subtilis ferrochelatase

2H1V の概要

• エントリーDOI: 10.2210/pdb2h1v/pdb
• 関連するPDBエントリー: 1DOZ 2AC2 2AC4 2H1W
• 分子名称: Ferrochelatase, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: rossmann fold, pi-helix, lyase
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cytoplasm: P32396
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35428.82

構造登録者

Hansson, M.D.,Karlberg, T.,Arys Rahardja, M.,Al-Karadaghi, S.,Hansson, M. (登録日: 2006-05-17, 公開日: 2007-01-16, 最終更新日: 2023-08-30)

主引用文献

Hansson, M.D.,Karlberg, T.,Rahardja, M.A.,Al-Karadaghi, S.,Hansson, M.
Amino Acid Residues His183 and Glu264 in Bacillus subtilis Ferrochelatase Direct and Facilitate the Insertion of Metal Ion into Protoporphyrin IX
Biochemistry, 46:87-94, 2007

PubMed Abstract: 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.

PubMed: 17198378
DOI: 10.1021/bi061760a

実験手法

X-RAY DIFFRACTION (1.2 Å)