Structural characterization and comparison of the large subunits of IPM isomerase and homoaconitase from Methanococcus jannaschii

IPM isomerase and homoaconitase belong to the aconitase family of enzymes and are composed of large and small subunits. The large subunits of the two enzymes adopt different active-site states before Fe-S cluster binding.

Structural basis of the heterodimerization of the MST and RASSF SARAH domains in the Hippo signalling pathway

The heterodimeric structure of the MST1 and RASSF5 SARAH domains is presented. A comparison of homodimeric and heterodimeric interactions provides a structural basis for the preferential association of the SARAH heterodimer.