3bs0

Crystal structure of the P. putida toluene transporter TodX

spinqualitylabelsall models 3bs0, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3bs0 is a 2 chain structure with sequence from Pseudomonas putida F1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: C8E Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A5W4F4_PSEP1 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 Bacterial biodegradation of hydrocarbons, an important process for environmental remediation, requires the passage of hydrophobic substrates across the cell membrane. Here, we report crystal structures of two outer membrane proteins, Pseudomonas putida TodX and Ralstonia pickettii TbuX, which have been implicated in hydrocarbon transport and are part of a subfamily of the FadL fatty acid transporter family. The structures of TodX and TbuX show significant differences with those previously determined for Escherichia coli FadL, which may provide an explanation for the substrate-specific transport of TodX and TbuX observed with in vivo transport assays. The TodX and TbuX structures revealed 14-stranded beta-barrels with an N-terminal hatch domain blocking the barrel interior. A hydrophobic channel with bound detergent molecules extends from the extracellular surface and is contiguous with a passageway through the hatch domain, lined by both hydrophobic and polar or charged residues. The TodX and TbuX structures support a mechanism for transport of hydrophobic substrates from the extracellular environment to the periplasm via a channel through the hatch domain. Outer-membrane transport of aromatic hydrocarbons as a first step in biodegradation.,Hearn EM, Patel DR, van den Berg B Proc Natl Acad Sci U S A. 2008 Jun 24;105(25):8601-6. Epub 2008 Jun 16. PMID:18559855 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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