3el6 | pdb_00003el6

Crystal Structure of the Erythromycin Dehydratase

spinqualitylabelsall models 3el6, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3el6 is a 1 chain structure with sequence from "actinomyces_erythreus"_(sic)_waksman_1923 "actinomyces erythreus" (sic) waksman 1923. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, SO4 Related: 2fr0, 2hg4 Gene: eryA ("Actinomyces erythreus" (sic) Waksman 1923) Activity: [acyl-carrier-protein_dehydratase 3-hydroxyacyl-[acyl-carrier-protein] dehydratase], with EC number 4.2.1.59 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 dehydratases (DHs) of modular polyketide synthases (PKSs) catalyze dehydrations that occur frequently in the biosynthesis of complex polyketides, yet little is known about them structurally or mechanistically. Here, the structure of a DH domain, isolated from the fourth module of the erythromycin PKS, is presented at 1.85 A resolution. As with the DH of the highly related animalian fatty acid synthase, the DH monomer possesses a double-hotdog fold. Two symmetry mates within the crystal lattice make a contact that likely represents the DH dimerization interface within an intact PKS. Conserved hydrophobic residues on the DH surface indicate potential interfaces with two other PKS domains, the ketoreductase and the acyl carrier protein. Mutation of an invariant arginine at the hypothesized acyl carrier protein docking site in the context of the erythromycin PKS resulted in decreased production of the erythromycin precursor 6-deoxyerythronolide B. The structure elucidates how the alpha-hydrogen and beta-hydroxyl group of a polyketide substrate interact with the catalytic histidine and aspartic acid in the DH active site prior to dehydration. Crystal structure of the erythromycin polyketide synthase dehydratase.,Keatinge-Clay A J Mol Biol. 2008 Dec 26;384(4):941-53. Epub 2008 Oct 11. PMID:18952099 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also 6-deoxyerythronolide B synthase (DEBS) 6-deoxyerythronolide B synthase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA