Crystal structure of the C-terminal domain of the plant-specific microtubule-associated protein Spiral2

In this study, the crystal structure of the conserved C-terminal domain of Spiral2 was determined using the single-wavelength anomalous dispersion method. Refinement of the model to a resolution of 2.2   Å revealed a helix – turn – helix fold with seven α -helices. The protein crystallized as a dimer, but SEC-MALS analysis showed the protein to be monomeric. A structural homology search revealed that the protein has similarity to the C-terminal domain of the katanin regulatory subunit p80. The structure presented here suggests that the C-terminal domain of Spiral2 represents a new class of microtubule dynamics modulator across the kingdom.

Source: Acta Crystallographica Section F - December 20, 2022 Category: Biochemistry Authors: Ohno, M. Higuchi, Y. Hayashi, I. Tags: microtubules Spiral2 plants Physcomitrella patens katanin research communications Source Type: research