Crystal structure of the C-terminal domain of the plant-specific microtubule-associated protein Spiral2.
Acta Crystallogr F Struct Biol Commun
; 79(Pt 1): 17-22, 2023 Jan 01.
Article
em En
| MEDLINE
| ID: mdl-36598352
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 2.2â
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.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Associadas aos Microtúbulos
/
Microtúbulos
Tipo de estudo:
Risk_factors_studies
Idioma:
En
Revista:
Acta Crystallogr F Struct Biol Commun
Ano de publicação:
2023
Tipo de documento:
Article