David Dotson

Open Force Field Initiative

Escherichia coli NhaA is a prototype sodium-proton antiporter, which has been extensively characterized by X-ray crystallography, biochemical and biophysical experiments. However, the identities of proton carriers and details of pH-regulated mechanism remain controversial. Here we report constant pH molecular dynamics data, which reveal that NhaA a...

In science the filesystem often serves as a de facto database, with directory trees being the zeroth-order scientific data structure. But it can be tedious and error prone to work directly with the filesystem to retrieve and store heterogeneous datasets. datreant makes working with directory structures and files Pythonic with Treants: specially mar...

MDAnalysis (http://mdanalysis.org) is a library for structural and temporal analysis of molecular dynamics (MD) simulation trajectories and individual protein structures. MD simulations of biological molecules have become an important tool to elucidate the relationship between molecular structure and physiological function. Simulations are performe...

To fully understand the transport mechanism of Na(+)/H(+) exchangers, it is necessary to clearly establish the global rearrangements required to facilitate ion translocation. Currently, two different transport models have been proposed. Some reports have suggested that structural isomerization is achieved through large elevator-like rearrangements...

Na+/H+ antiporters are vital for maintaining homeostasis in bacterial cells, in particular for survival in high-salt environments. In humans, these transporters are important drug targets, because their dysfunction is linked to a variety of diseases, including cancer and cardiovascular pathophysiology. However, to date the molecular mechanism by wh...

Na þ /H þ antiporters are vital to cells for maintaining homeostasis, especially in high-salt environments. New crystal structures for two such antiporters, cytoplasmic-open Escherichia coli NhaA and periplasmic-open Thermus Thermophilus NapA, show high structural similarity despite low sequence identity. Among their common features are a set of hi...

Sodium-proton antiporters rapidly exchange protons and sodium ions across the membrane to regulate intracellular pH, cell volume, and sodium concentration. How ion binding and release is coupled to the conformational changes associated with transport is not clear. Here, we report a crystal form of the prototypical sodium-proton antiporter NhaA from...

Sodium/proton (Na+/H+) antiporters, located at the plasma membrane in every cell, are vital for cell homeostasis. In humans, their dysfunction has been linked to diseases, such as hypertension, heart failure and epilepsy, and they are well-established drug targets. The best understood model system for Na+/H+ antiport is NhaA from Escherichia coli,...