Dimeric Sfh3 has structural changes in its binding pocket that are associated with a dimer-monomer state transformation induced by substrate binding

The dimeric structure of Sfh3 (Sec14 family homologue 3 in yeast) is reported for the first time and differs from the Sec14 proteins reported to date, all of which are monomeric.

Structures of enzyme–intermediate complexes of yeast Nit2: insights into its catalytic mechanism and different substrate specificity compared with mammalian Nit2

Structures of yeast Nit2 in complex with α-ketoglutarate and with oxaloacetate revealed the molecular-recognition mechanism of the enzyme for the first time, while that of the C169S mutant of yeast Nit2 showed a new ligand located in the catalytic cavity.

Cross-protomer interaction with the photoactive site in oligomeric proteorhodopsin complexes

The first crystal structure of a proteorhodopsin shows a hexametric ring of protein in which the conserved photoactive-site histidine forms a hydrogen bond to the Schiff base proton acceptor from the same molecule and also to a tryptophan residue of a neighboring protomer. The structure and mutant studies reveal novel aspects of the ion translocation mechanism and cooperative behavior between protomers involving the inter-molecular His-Trp pair.