The Spatial and Temporal Evolution of the Portland and Tualatin Forearc Basins, Oregon, USA

The Portland and Tualatin basins are part of the Salish-Puget-Willamette Lowland, a 900-km-long, forearc depression lying between the volcanic arc and the Coast Ranges of the Cascadia convergent margin. Such inland seaways are characteristic of warm, young slab subduction. We analyzed the basins to better understand their evolution and relation to Coast Range history and to provide an improved tectonic framework for the Portland metropolitan area. We model three key horizons in the basins: (1) the top of the Columbia River Basalt Group (CRBG), (2) the bottom of the CRBG, and (3) the top of Eocene basement. Isochore maps constrain basin depocenters during (1) Pleistocene to mid-Miocene time (0–15 Ma), (2) CRBG (15.5–16.5 Ma), and (3) early Miocene to late Eocene (ca. 17–35 Ma) time. Results show that the Portland and Tualatin basins have distinct mid-Miocene to Quaternary depocenters but were one continuous basin from the Eocene until mid-Miocene time. A NW-striking gravity low coincident with the NW-striking, fault-bounded Portland Hills anticline is interpreted as an older graben coincident with observed thickening of CRBG flows and underlying sedimentary rocks. Neogene transpression in the forearc structurally inverted the Sylvan-Oatfield and Portland Hills normal faults as high-angle dextral-reverse faults, separating the Portland and Tualatin basins. An eastward shift of the forearc basin depocenter and ten-fold decrease in accommodation space provide temporal constraints on the emergence of the Coast Range to the west. Clockwise rotation and northward transport of the forearc is deforming the basins and producing local earthquakes beneath the metropolitan area

The structure of the bacterial oxidoreductase enzyme DsbA in complex with a peptide reveals a basis for substrate specificity in the catalytic cycle of DsbA enzymes

Oxidative protein folding in Gram-negative bacteria results in the formation of disulfide bonds between pairs of cysteine residues. This is a multistep process in which the dithiol-disulfide oxidoreductase enzyme, DsbA, plays a central role. The structure of DsbA comprises an all helical domain of unknown function and a thioredoxin domain, where active site cysteines shuttle between an oxidized, substrate-bound, reduced form and a DsbB-bound form, where DsbB is a membrane protein that reoxidizes DsbA. Most DsbA enzymes interact with a wide variety of reduced substrates and show little specificity. However, a number of DsbA enzymes have now been identified that have narrow substrate repertoires and appear to interact specifically with a smaller number of substrates. The transient nature of the DsbA-substrate complex has hampered our understanding of the factors that govern the interaction of DsbA enzymes with their substrates. Here we report the crystal structure of a complex between Escherichia coli DsbA and a peptide with a sequence derived from a substrate. The binding site identified in the DsbA-peptide complex was distinct from that observed for DsbB in the DsbA-DsbB complex. The structure revealed details of the DsbA-peptide interaction and suggested a mechanism by which DsbA can simultaneously show broad specificity for substrates yet exhibit specificity for DsbB. This mode of binding was supported by solution nuclear magnetic resonance data as well as functional data, which demonstrated that the substrate specificity of DsbA could be modified via changes at the binding interface identified in the structure of the comple

DSB proteins and bacterial pathogenicity

If DNA is the information of life, then proteins are the machines of life — but they must be assembled and correctly folded to function. A key step in the protein-folding pathway is the introduction of disulphide bonds between cysteine residues in a process called oxidative protein folding. Many bacteria use an oxidative protein-folding machinery to assemble proteins that are essential for cell integrity and to produce virulence factors. Although our current knowledge of this machinery stems largely from Escherichia coli K-12, this view must now be adjusted to encompass the wider range of disulphide catalytic systems present in bacteria