2qd2 | pdb_00002qd2

F110A variant of human ferrochelatase with protoheme bound

spinqualitylabelsall models 2qd2, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2qd2 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BCT, CHD, FES, HEM, IMD Gene: DKFZp686P18130 (HUMAN) Activity: Ferrochelatase, with EC number 4.99.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [Q7KZA3_HUMAN] Catalyzes the ferrous insertion into protoporphyrin IX (By similarity).[RuleBase:RU000607] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ferrochelatase

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