4nxl

Dibenzothiophene monooxygenase (DszC) from Rhodococcus erythropolis

spinqualitylabelsall models 4nxl, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4nxl is a 4 chain structure with sequence from Rhodococcus erythropolis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DSZC3_RHOER Catalyzes the first step of the '4S' desulfurization pathway that removes covalently bound sulfur from dibenzothiophene (DBT) without breaking carbon-carbon bonds. Sulfur dioxygenase which converts DBT to DBT-sulfone (DBTO2 or DBT 5,5-dioxide) in a stepwise manner. Publication Abstract from PubMed Dibenzothiophene (DBT) is a typical sulfur-containing compound found in fossil fuels. This compound and its derivatives are resistant to the hydrodesulfurization method often used in industry, but they are susceptible to enzymatic desulfurization via the 4S pathway, which is a well-studied biochemical pathway consisting of four enzymes. DBT monooxygenase (DszC) from Rhodococcus erythropolis is involved in the first step of the 4S pathway. We determined the crystal structure of DszC, which reveals that, in contrast to several homologous proteins, the C-terminus (410-417) of DszC participates in the stabilization of the substrate-binding pocket. Analytical ultracentrifugation analysis and enzymatic assays confirmed that the C-terminus is important for the stabilization of the active conformation of the substrate-binding pocket and the tetrameric state. Therefore, the C-terminus of DszC plays a significant role in the catalytic activity of this enzyme. Proteins 2014. (c) 2014 Wiley Periodicals, Inc. Structural insights into the stabilization of active, tetrameric DszC by its C-terminus.,Zhang L, Duan X, Zhou D, Dong Z, Ji K, Meng W, Li G, Li X, Yang H, Ma T, Rao Z Proteins. 2014 Jun 28. doi: 10.1002/prot.24638. PMID:24975806 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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