8HBR

The C-terminal domain of Spiral2

Summary for 8HBR

• Entry DOI: 10.2210/pdb8hbr/pdb
• Descriptor: TOG domain-containing protein (2 entities in total)
• Functional Keywords: microtubule associated protein, structural protein
• Biological source: Physcomitrium patens
• Total number of polymer chains: 6
• Total formula weight: 91220.31

Authors

Hayashi, I. (deposition date: 2022-10-30, release date: 2023-01-18, Last modification date: 2024-10-09)

Primary citation

Ohno, M.,Higuchi, Y.,Hayashi, I.
Crystal structure of the C-terminal domain of the plant-specific microtubule-associated protein Spiral2.
Acta Crystallogr.,Sect.F, 79:17-22, 2023

PubMed Abstract: Plant cells form microtubule arrays, called `cortical microtubules', beneath the plasma membrane which are critical for cell-wall organization and directional cell growth. Cortical microtubules are nucleated independently of centrosomes. Spiral2 is a land-plant-specific microtubule minus-end-targeting protein that stabilizes the minus ends by inhibiting depolymerization of the filament. Spiral2 possesses an N-terminal microtubule-binding domain and a conserved C-terminal domain whose function is unknown. 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.

PubMed: 36598352
DOI: 10.1107/S2053230X22011815

Experimental method

X-RAY DIFFRACTION (2.2 Å)