X-ray structures of eIF5B and the eIF5B-eIF1A complex: the conformational flexibility of eIF5B is restricted on the ribosome by interaction with eIF1A

Two crystal forms of eIF5B and one crystal form of the eIF5B-eIF1A complex exhibit four different conformations of eIF5B, indicating that the conformation of eIF5B is highly flexible. The interaction between eIF5B domain IV and the eIF1A C-terminal tail may restrict the flexibility of eIF5B on the ribosome and stabilize the interface for ribosome subunit joining.

Structures of AzrA and of AzrC complexed with substrate or inhibitor: insight into substrate specificity and catalytic mechanism

The reduction reactions of different substrates by azoreductases have been investigated based on the crystal structures of AzrA and of AzrC–inhibitor/substrate complexes. The structures of the AzrC–substrate complexes present two different manners of binding, suggesting two types of reduction reaction depending on the type of substrate.