2hre: Difference between revisions
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[[Image:2hre.jpg|left|200px]] | [[Image:2hre.jpg|left|200px]] | ||
'''Structure of human ferrochelatase variant E343K with protoporphyrin IX bound''' | {{Structure | ||
|PDB= 2hre |SIZE=350|CAPTION= <scene name='initialview01'>2hre</scene>, resolution 2.50Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=PP9:PROTOPORPHYRIN+IX'>PP9</scene>, <scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene> and <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] | |||
|GENE= FECH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Structure of human ferrochelatase variant E343K with protoporphyrin IX bound''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2HRE is a [ | 2HRE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HRE OCA]. | ||
==Reference== | ==Reference== | ||
Substrate interactions with human ferrochelatase., Medlock A, Swartz L, Dailey TA, Dailey HA, Lanzilotta WN, Proc Natl Acad Sci U S A. 2007 Feb 6;104(6):1789-93. Epub 2007 Jan 29. PMID:[http:// | Substrate interactions with human ferrochelatase., Medlock A, Swartz L, Dailey TA, Dailey HA, Lanzilotta WN, Proc Natl Acad Sci U S A. 2007 Feb 6;104(6):1789-93. Epub 2007 Jan 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17261801 17261801] | ||
[[Category: Ferrochelatase]] | [[Category: Ferrochelatase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: protoporphyrin ix]] | [[Category: protoporphyrin ix]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:20:35 2008'' | ||
Revision as of 18:20, 20 March 2008
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| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Gene: | FECH (Homo sapiens) | ||||||
| Activity: | Ferrochelatase, with EC number 4.99.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of human ferrochelatase variant E343K with protoporphyrin IX bound
OverviewOverview
Ferrochelatase, the terminal enzyme in heme biosynthesis, catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme IX. Human ferrochelatase is a homodimeric, inner mitochondrial membrane-associated enzyme that possesses an essential [2Fe-2S] cluster. In this work, we report the crystal structure of human ferrochelatase with the substrate protoporphyrin IX bound as well as a higher resolution structure of the R115L variant without bound substrate. The data presented reveal that the porphyrin substrate is bound deep within an enclosed pocket. When compared with the location of N-methylmesoporphyrin in the Bacillus subtilis ferrochelatase, the porphyrin is rotated by approximately 100 degrees and is buried an additional 4.5 A deeper within the active site. The propionate groups of the substrate do not protrude into solvent and are bound in a manner similar to what has been observed in uroporphyrinogen decarboxylase. Furthermore, in the substrate-bound form, the jaws of the active site mouth are closed so that the porphyrin substrate is completely engulfed in the pocket. These data provide insights that will aid in the determination of the mechanism for ferrochelatase.
DiseaseDisease
Known diseases associated with this structure: Protoporphyria, erythropoietic OMIM:[177000], Protoporphyria, erythropoietic, recessive, with liver failure OMIM:[177000]
About this StructureAbout this Structure
2HRE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Substrate interactions with human ferrochelatase., Medlock A, Swartz L, Dailey TA, Dailey HA, Lanzilotta WN, Proc Natl Acad Sci U S A. 2007 Feb 6;104(6):1789-93. Epub 2007 Jan 29. PMID:17261801
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