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 Cited by 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: 36598352DOI: 10.1107/S2053230X22011815 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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