2rds | pdb_00002rds

Crystal Structure of PtlH with Fe/oxalylglycine and ent-1-deoxypentalenic acid bound

spinqualitylabelsall models 2rds, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2rds is a 1 chain structure with sequence from "streptomyces_avermitilis"_burg_et_al._1979 "streptomyces avermitilis" burg et al. 1979. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 1PL, FE, MG, OGA Related: 2rdn, 2rdq, 2rdr Gene: ptlH ("Streptomyces avermitilis" Burg et al. 1979) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PTLH_STRAW] Catalyzes the conversion of 1-deoxypentalenic acid to 11-beta-hydroxy-1-deoxypentalenic acid in the biosynthesis of neopentalenolactone antibiotic. 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 The non-heme iron dioxygenase PtlH from the soil organism Streptomyces avermitilis is a member of the iron(II)/alpha-ketoglutarate-dependent dioxygenase superfamily and catalyzes an essential reaction in the biosynthesis of the sesquiterpenoid antibiotic pentalenolactone. To investigate the structural basis for substrate recognition and catalysis, we have determined the x-ray crystal structure of PtlH in several complexes with the cofactors iron, alpha-ketoglutarate, and the non-reactive enantiomer of the substrate, ent-1-deoxypentalenic acid, in four different crystal forms to up to 1.31 A resolution. The overall structure of PtlH forms a double-stranded barrel helix fold, and the cofactor-binding site for iron and alpha-ketoglutarate is similar to other double-stranded barrel helix fold enzymes. Additional secondary structure elements that contribute to the substrate-binding site in PtlH are not conserved in other double-stranded barrel helix fold enzymes. Binding of the substrate enantiomer induces a reorganization of the monoclinic crystal lattice leading to a disorder-order transition of a C-terminal alpha-helix. The newly formed helix blocks the major access to the active site and effectively traps the bound substrate. Kinetic analysis of wild type and site-directed mutant proteins confirms a critical function of two arginine residues in substrate binding, while simulated docking of the enzymatic reaction product reveals the likely orientation of bound substrate. Crystal structure of the non-heme iron dioxygenase PtlH in pentalenolactone biosynthesis.,You Z, Omura S, Ikeda H, Cane DE, Jogl G J Biol Chem. 2007 Dec 14;282(50):36552-60. Epub 2007 Oct 16. PMID:17942405 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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