1HRK

CRYSTAL STRUCTURE OF HUMAN FERROCHELATASE

Summary for 1HRK

• Entry DOI: 10.2210/pdb1hrk/pdb
• Descriptor: FERROCHELATASE, CHOLIC ACID, FE2/S2 (INORGANIC) CLUSTER, ... (4 entities in total)
• Functional Keywords: ferrochelatase, fe2s2 cluster, heme biosynthesis, protoheme ferro-lyase, mature length, proteolytically processed mitochondrial inner membrane protein, lyase
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side: P22830
• Total number of polymer chains: 2
• Total formula weight: 85071.76

Authors

Wu, C.K.,Dailey, H.A.,Rose, J.P.,Burden, A.,Sellers, V.M.,Wang, B.-C. (deposition date: 2000-12-21, release date: 2001-06-22, Last modification date: 2024-02-07)

Primary citation

Wu, C.K.,Dailey, H.A.,Rose, J.P.,Burden, A.,Sellers, V.M.,Wang, B.C.
The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis.
Nat.Struct.Biol., 8:156-160, 2001

PubMed Abstract: Human ferrochelatase (E.C. 4.99.1.1) is a homodimeric (86 kDa) mitochondrial membrane-associated enzyme that catalyzes the insertion of ferrous iron into protoporphyrin to form heme. We have determined the 2.0 A structure from the single wavelength iron anomalous scattering signal. The enzyme contains two NO-sensitive and uniquely coordinated [2Fe-2S] clusters. Its membrane association is mediated in part by a 12-residue hydrophobic lip that also forms the entrance to the active site pocket. The positioning of highly conserved residues in the active site in conjunction with previous biochemical studies support a catalytic model that may have significance in explaining the enzymatic defects that lead to the human inherited disease erythropoietic protoporphyria.

PubMed: 11175906
DOI: 10.1038/84152

Experimental method

X-RAY DIFFRACTION (2 Å)