issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

March 2026 issue

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Cover illustration: The structure of a chimeric protein, MexBYB, obtained by replacing the funnel-like and transmembrane domains of the RND-type multidrug-efflux pump MexY with those of the homologous transporter MexB, was determined by cryoEM under apo and kanamycin-supplemented conditions [Wang et al. (2026), Acta Cryst. F82, 83–93]. Under both conditions, MexBYB was reported to adopt symmetric-like and asymmetric conformations.

early career research


research communications


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This report describes the crystallization and X-ray structure of a highly aggregation-prone monobody engineered for small-molecule recognition. By employing a maltose-binding protein fusion strategy with optimized inter-domain linkers, we successfully obtained diffraction-quality crystals of the protein–ligand complex and determined its structure.

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In this study, cryo-EM structures of the chimeric RND transporter MexBYB, composed of MexB and MexY, are presented, revealing distinct symmetric-like and asymmetric conformations under apo and drug-supplemented conditions. These structures show that the unusually large open clefts observed in MexBYB, similar to those in MexY, represent a unique conformational feature of the MexY porter domain.

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Structural analysis of the GH85 enzyme endo-β-N-acetylglucosaminidase HSα reveals a novel domain that is potentially involved in complex N-glycan recognition.
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