2qd2
From Proteopedia
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|PDB= 2qd2 |SIZE=350|CAPTION= <scene name='initialview01'>2qd2</scene>, resolution 2.20Å | |PDB= 2qd2 |SIZE=350|CAPTION= <scene name='initialview01'>2qd2</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</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= DKFZp686P18130 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= DKFZp686P18130 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qd2 OCA], [http://www.ebi.ac.uk/pdbsum/2qd2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qd2 RCSB]</span> | ||
}} | }} | ||
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[[Category: Medlock, A E.]] | [[Category: Medlock, A E.]] | ||
[[Category: Ross, T A.]] | [[Category: Ross, T A.]] | ||
| - | [[Category: BCT]] | ||
| - | [[Category: CHD]] | ||
| - | [[Category: FES]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: IMD]] | ||
[[Category: biosynthetic protein]] | [[Category: biosynthetic protein]] | ||
[[Category: ferrochelatase]] | [[Category: ferrochelatase]] | ||
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[[Category: protoporphyrin ix]] | [[Category: protoporphyrin ix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:47:51 2008'' |
Revision as of 01:47, 31 March 2008
| |||||||
| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Gene: | DKFZp686P18130 (Homo sapiens) | ||||||
| Activity: | Ferrochelatase, with EC number 4.99.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
F110A variant of human ferrochelatase with protoheme bound
Overview
Ferrochelatase (protoheme ferrolyase, EC 4.99.1.1) is the terminal enzyme in heme biosynthesis and catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme IX (heme). Due to the many critical roles of heme, synthesis of heme is required by the vast majority of organisms. Despite significant investigation of both the microbial and eukaryotic enzyme, details of metal chelation remain unidentified. Here we present the first structure of the wild-type human enzyme, a lead-inhibited intermediate of the wild-type enzyme with bound metallated porphyrin macrocycle, the product bound form of the enzyme, and a higher resolution model for the substrate-bound form of the E343K variant. These data paint a picture of an enzyme that undergoes significant changes in secondary structure during the catalytic cycle. The role that these structural alterations play in overall catalysis and potential protein-protein interactions with other proteins, as well as the possible molecular basis for these changes, is discussed. The atomic details and structural rearrangements presented herein significantly advance our understanding of the substrate binding mode of ferrochelatase and reveal new conformational changes in a structurally conserved pi-helix that is predicted to have a central role in product release.
About this Structure
2QD2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase., Medlock AE, Dailey TA, Ross TA, Dailey HA, Lanzilotta WN, J Mol Biol. 2007 Nov 2;373(4):1006-16. Epub 2007 Aug 23. PMID:17884090
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