Cédric Orelle

This study reports the crystal and cryo-EM structures of Streptococcus pneumoniae NDK, revealing its hexameric form and higher-order supramolecular assemblies, and suggests these structures may modulate its function.

The paper identifies a conserved residue cluster in BmrA that mediates communication between nucleotide and substrate binding sites in type IV ABC transporters through coupling helix 2.

This study shows that Rhodamine6G binding to BmrA narrows its conformational spectrum, enhancing ATP-dependent transport efficiency.