Browse by author
Lookup NU author(s): Dr Sven Halbedel, Professor Rick Lewis
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
© 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.
Author(s): Halbedel S, Lewis RJ
Publication type: Review
Publication status: Published
Journal: Molecular Microbiology
Year: 2019
Volume: 111
Issue: 6
Pages: 1404-1415
Print publication date: 12/06/2019
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
