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1hrk
From Proteopedia
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[[Image:1hrk.gif|left|200px]] | [[Image:1hrk.gif|left|200px]] | ||
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'''CRYSTAL STRUCTURE OF HUMAN FERROCHELATASE''' | '''CRYSTAL STRUCTURE OF HUMAN FERROCHELATASE''' | ||
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[[Category: Wang, B C.]] | [[Category: Wang, B C.]] | ||
[[Category: Wu, C K.]] | [[Category: Wu, C K.]] | ||
| - | [[Category: | + | [[Category: Fe2s2 cluster]] |
| - | [[Category: | + | [[Category: Ferrochelatase]] |
| - | [[Category: | + | [[Category: Heme biosynthesis]] |
| - | [[Category: | + | [[Category: Mature length]] |
| - | [[Category: | + | [[Category: Proteolytically processed mitochondrial inner membrane protein]] |
| - | [[Category: | + | [[Category: Protoheme ferro-lyase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:09:48 2008'' | |
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Revision as of 16:09, 2 May 2008
CRYSTAL STRUCTURE OF HUMAN FERROCHELATASE
Overview
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.
About this Structure
1HRK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis., Wu CK, Dailey HA, Rose JP, Burden A, Sellers VM, Wang BC, Nat Struct Biol. 2001 Feb;8(2):156-60. PMID:11175906 Page seeded by OCA on Fri May 2 19:09:48 2008
