Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6OMP

Crystal structure of apo PtmU3

Summary for 6OMP
Entry DOI10.2210/pdb6omp/pdb
DescriptorPtmU3, ACETATE ION, MANGANESE (II) ION, ... (4 entities in total)
Functional Keywordstim-barrel, oxidoreductase
Biological sourceStreptomyces platensis
Total number of polymer chains2
Total formula weight79800.40
Authors
Liu, Y.C.,Dong, L.B.,Shen, B. (deposition date: 2019-04-19, release date: 2019-07-24, Last modification date: 2024-03-13)
Primary citationDong, L.B.,Liu, Y.C.,Cepeda, A.J.,Kalkreuter, E.,Deng, M.R.,Rudolf, J.D.,Chang, C.,Joachimiak, A.,Phillips Jr., G.N.,Shen, B.
Characterization and Crystal Structure of a Nonheme Diiron Monooxygenase Involved in Platensimycin and Platencin Biosynthesis.
J.Am.Chem.Soc., 141:12406-12412, 2019
Cited by
PubMed Abstract: Nonheme diiron monooxygenases make up a rapidly growing family of oxygenases that are rarely identified in secondary metabolism. Herein, we report the in vivo, in vitro, and structural characterizations of a nonheme diiron monooxygenase, PtmU3, that installs a C-5 β-hydroxyl group in the unified biosynthesis of platensimycin and platencin, two highly functionalized diterpenoids that act as potent and selective inhibitors of bacterial and mammalian fatty acid synthases. This hydroxylation sets the stage for the subsequent A-ring cleavage step key to the unique diterpene-derived scaffolds of platensimycin and platencin. PtmU3 adopts an unprecedented triosephosphate isomerase (TIM) barrel structural fold for this class of enzymes and possesses a noncanonical diiron active site architecture with a saturated six-coordinate iron center lacking a μ-oxo bridge. This study reveals the first member of a previously unidentified superfamily of TIM-barrel-fold enzymes for metal-dependent dioxygen activation, with the majority predicted to act on CoA-linked substrates, thus expanding our knowledge of nature's repertoire of nonheme diiron monooxygenases and TIM-barrel-fold enzymes.
PubMed: 31291107
DOI: 10.1021/jacs.9b06183
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

237735

数据于2025-06-18公开中

PDB statisticsPDBj update infoContact PDBjnumon