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

doi:10.1038/s42003-022-03054-z

Communications Biology (May 2022)

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

Affiliations

Shifra Lansky: Institute of Chemistry, the Hebrew University of Jerusalem
Rachel Salama: Department of Biotechnology and Food Engineering, Technion
Xevi Biarnés: Laboratory of Biochemistry, Institut Químic de Sarrià, Universitat Ramon Llull
Omer Shwartstein: Institute of Chemistry, the Hebrew University of Jerusalem
Dina Schneidman-Duhovny: School of Computer Science and Engineering, the Hebrew University of Jerusalem
Antoni Planas: Laboratory of Biochemistry, Institut Químic de Sarrià, Universitat Ramon Llull
Yuval Shoham: Department of Biotechnology and Food Engineering, Technion
Gil Shoham: Institute of Chemistry, the Hebrew University of Jerusalem

DOI: https://doi.org/10.1038/s42003-022-03054-z
Journal volume & issue: Vol. 5, no. 1
pp. 1 – 14

Abstract

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Lansky et al. describe the structural analysis of an ultra-multimodular GH43 arabinanase, AbnA. They discover a new carbohydrate binding module and analyze the large conformational transitions of the enzyme with the integrative structure determination approach, which may be applied to the conformational studies of other ultramultimodular proteins as well.

Published in Communications Biology

ISSN: 2399-3642 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science: Biology (General)
Website: https://www.nature.com/commsbio/

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