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Structural basis for interaction of DivIVA/GpsB proteins with their ligands

Lookup NU author(s): Dr Sven Halbedel, Professor Rick Lewis

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Abstract

© 2019 John Wiley & Sons Ltd DivIVA proteins and their GpsB homologues are late cell division proteins found in Gram-positive bacteria. DivIVA/GpsB proteins associate with the inner leaflet of the cytosolic membrane and act as scaffolds for other proteins required for cell growth and division. DivIVA/GpsB proteins comprise an N-terminal lipid-binding domain for membrane association fused to C-terminal domains supporting oligomerization. Despite sharing the same domain organization, DivIVA and GpsB serve different cellular functions: DivIVA plays diverse roles in division site selection, chromosome segregation and controlling peptidoglycan homeostasis, whereas GpsB contributes to the spatiotemporal control of penicillin-binding protein activity. The crystal structures of the lipid-binding domains of DivIVA from Bacillus subtilis and GpsB from several species share a fold unique to this group of proteins, whereas the C-terminal domains of DivIVA and GpsB are radically different. A number of pivotal features identified from the crystal structures explain the functional differences between the proteins. Herein we discuss these structural and functional relationships and recent advances in our understanding of how DivIVA/GpsB proteins bind and recruit their interaction partners, knowledge that might be useful for future structure-based DivIVA/GpsB inhibitor design.


Publication metadata

Author(s): Halbedel S, Lewis RJ

Publication type: Review

Publication status: Published

Journal: Molecular Microbiology

Year: 2019

Pages: Epub ahead of print

Online publication date: 18/03/2019

Acceptance date: 13/03/2019

ISSN (print): 0950-382X

ISSN (electronic): 1365-2958

Publisher: Blackwell Publishing Ltd

URL: https://doi.org/10.1111/mmi.14244

DOI: 10.1111/mmi.14244

PubMed id: 30887576


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