1hrk: Difference between revisions

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[[Image:1hrk.gif|left|200px]]
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[[Image:1hrk.png|left|200px]]


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{{STRUCTURE_1hrk|  PDB=1hrk  |  SCENE=  }}  
{{STRUCTURE_1hrk|  PDB=1hrk  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF HUMAN FERROCHELATASE'''
===CRYSTAL STRUCTURE OF HUMAN FERROCHELATASE===




==Overview==
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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.
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{{ABSTRACT_PUBMED_11175906}}


==About this Structure==
==About this Structure==
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[[Category: Proteolytically processed mitochondrial inner membrane protein]]
[[Category: Proteolytically processed mitochondrial inner membrane protein]]
[[Category: Protoheme ferro-lyase]]
[[Category: Protoheme ferro-lyase]]
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Revision as of 05:35, 1 July 2008

File:1hrk.png

Template:STRUCTURE 1hrk

CRYSTAL STRUCTURE OF HUMAN FERROCHELATASE

Template:ABSTRACT PUBMED 11175906

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

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