Burak V. Kabasakal

This study analyzes the structural heterogeneity of uncrosslinked FtsH-HflKC complexes using cryo-EM and SAXS, revealing variable FtsH occupancy and a distinct wild-type FtsH architecture.

The paper reports cryo-EM structures of the Escherichia coli FtsH periplasmic domain, revealing conformational flexibility and its role in substrate translocation.

The paper uses cryo-EM to analyze membrane proteins, revealing unexpected high-resolution structures of ArnA and AcrB instead of the intended FtsH and YidC complex.

The paper reinterprets the crystal structure of FeSII from Azotobacter vinelandii, proposing a domain swap rather than an open conformation due to oxidation state.

The paper reveals how CP12 regulates the Calvin cycle by structurally pre-ordering itself before binding PRK and influencing GAPDH activity based on redox state and NAD availability.