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

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