A phage-encoded protein inhibits a bacterial replicative helicase loading factor by exploiting an internal site that auto-regulates loader self-assembly and ATPase activity.

Solid state NMR is unable to detect any association of substrate to the second binding site, S2, in the extracellular vestibule of the Neurotransmitter:Sodium Symporter LeuT.

Co-evolving residue pairs in the different components of a protein complex almost always make contact across the protein–protein interface, thus providing powerful restraints for the modeling of protein complexes.

Analysis of the Escherichia coli DnaB helicase•bacteriophage λ helicase loader (λP) complex provides insights into helicase opening, delivery to the origin and ssDNA entry, and closing in preparation for translocation.

Differences in HDR product preference present a novel mechanism in plants to control substrate availability for short- and long-chain isoprenoids.

The genome of Thermovibrio ammonificans encodes ancestral pathways (e.g., hydrogen oxidation) and more recently acquired ones (e.g., nitrate reduction) and a hybrid pathway for CO₂ fixation.

Evolutionary bioinformatics and experimentation are applied to the components of the Tat protein transport system to elucidate the structure of the membrane-bound receptor complex and to deduce a molecular description for its substrate-triggered activation.

An unexpected new biological function was discovered for the universally conserved cofactor lipoate, as lipoate-binding proteins proved essential for a novel wide-spread prokaryotic sulfur oxidation pathway.

Mutational analysis and biochemical experiments suggest that the conserved β-hairpin-like membrane-reentrant loop of RseP - an S2P family intramembrane cleaving protease - helps to discriminate substrates by directly interacting with their transmembrane segments.

Many bacteria use the Nus factor antitermination complex to prevent premature Rho-dependent transcription termination of their CRISPR arrays.