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1hrk
From Proteopedia
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|PDB= 1hrk |SIZE=350|CAPTION= <scene name='initialview01'>1hrk</scene>, resolution 2.00Å | |PDB= 1hrk |SIZE=350|CAPTION= <scene name='initialview01'>1hrk</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene> | + | |LIGAND= <scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hrk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hrk OCA], [http://www.ebi.ac.uk/pdbsum/1hrk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hrk RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: Protoporphyria, erythropoietic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=177000 177000]], Protoporphyria, erythropoietic, recessive, with liver failure OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=177000 177000]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Wang, B C.]] | [[Category: Wang, B C.]] | ||
[[Category: Wu, C K.]] | [[Category: Wu, C K.]] | ||
| - | [[Category: CHD]] | ||
| - | [[Category: FES]] | ||
[[Category: fe2s2 cluster]] | [[Category: fe2s2 cluster]] | ||
[[Category: ferrochelatase]] | [[Category: ferrochelatase]] | ||
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[[Category: protoheme ferro-lyase]] | [[Category: protoheme ferro-lyase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:09:30 2008'' |
Revision as of 18:09, 30 March 2008
| |||||||
| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Ferrochelatase, with EC number 4.99.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 21:09:30 2008
