Feng Long

TL;DR: The crystal structure indicates that CusA has, in addition to the three-methionine metal-binding site, four methionine pairs—three located in the transmembrane region and one in the periplasmic domain, which directly suggests a plausible pathway for ion export.

TL;DR: The co-crystal structure of the CusBA efflux complex is reported, showing that the transporter (or pump) CusA, which is present as a trimer, interacts with six CusB protomers and that the periplasmic domain of CUSA is involved in these interactions.

TL;DR: It is determined that broadly neutralizing MAbs block multiple steps in the viral lifecycle, including entry and egress, and bind to a conserved epitope on the B domain of the E2 glycoprotein.

TL;DR: In this paper, the crystal structures of EV-D68 and its complex with pleconaril, a capsid-binding compound that had been developed as an anti-rhinovirus drug, were reported.

TL;DR: AdpAc, an S. coelicolor gene similar to the Streptomyces griseus A factor‐regulated adpAg, was found to complement the bldH109 mutant partially at both single and multiple copies, and revealed that translational arrest at the UUA codon in adpAc mRNA is the principal target through which bldA influences morphological differentiation.