Integrative structure determination reveals functional global flexibility for an ultra-multimodular arabinanase

Shifra Lansky, Rachel Salama, Xevi Biarnés, Omer Shwartstein, Dina Schneidman-Duhovny, Antoni Planas, Yuval Shoham, Gil Shoham

Producción científica: Artículo en revista indizadaArtículorevisión exhaustiva

3 Citas (Scopus)

Resumen

AbnA is an extracellular GH43 α-L-arabinanase from Geobacillus stearothermophilus, a key bacterial enzyme in the degradation and utilization of arabinan. We present herein its full-length crystal structure, revealing the only ultra-multimodular architecture and the largest structure to be reported so far within the GH43 family. Additionally, the structure of AbnA appears to contain two domains belonging to new uncharacterized carbohydrate-binding module (CBM) families. Three crystallographic conformational states are determined for AbnA, and this conformational flexibility is thoroughly investigated further using the “integrative structure determination” approach, integrating molecular dynamics, metadynamics, normal mode analysis, small angle X-ray scattering, dynamic light scattering, cross-linking, and kinetic experiments to reveal large functional conformational changes for AbnA, involving up to ~100 Å movement in the relative positions of its domains. The integrative structure determination approach demonstrated here may apply also to the conformational study of other ultra-multimodular proteins of diverse functions and structures.

Idioma originalInglés
Número de artículo465
PublicaciónCommunications Biology
Volumen5
N.º1
DOI
EstadoPublicada - dic 2022

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