4UG1

GpsB N-terminal domain

Summary for 4UG1

• Entry DOI: 10.2210/pdb4ug1/pdb
• Related: 4UG3
• Descriptor: CELL CYCLE PROTEIN GPSB, NICKEL (II) ION, IMIDAZOLE, ... (4 entities in total)
• Functional Keywords: cell cycle, peptidoglycan synthesis, bacterial cell division, bacterial growth regulation
• Biological source: LISTERIA MONOCYTOGENES
• Total number of polymer chains: 2
• Total formula weight: 17853.34

Authors

Rismondo, J.,Cleverley, R.M.,Lane, H.V.,Grohennig, S.,Steglich, A.,Muller, L.,Krishna Mannala, G.,Hain, T.,Lewis, R.J.,Halbedel, S. (deposition date: 2015-03-20, release date: 2015-11-25, Last modification date: 2023-12-20)

Primary citation

Rismondo, J.,Cleverley, R.M.,Lane, H.V.,Grosshennig, S.,Steglich, A.,Moller, L.,Mannala, G.K.,Hain, T.,Lewis, R.J.,Halbedel, S.
Structure of the Bacterial Cell Division Determinant Gpsb and its Interaction with Penicillin Binding Proteins.
Mol.Microbiol., 99:978-, 2016

PubMed Abstract: Each bacterium has to co-ordinate its growth with division to ensure genetic stability of the population. Consequently, cell division and growth are tightly regulated phenomena, albeit different bacteria utilise one of several alternative regulatory mechanisms to maintain control. Here we consider GpsB, which is linked to cell growth and division in Gram-positive bacteria. ΔgpsB mutants of the human pathogen Listeria monocytogenes show severe lysis, division and growth defects due to distortions of cell wall biosynthesis. Consistent with this premise, GpsB interacts both in vitro and in vivo with the major bi-functional penicillin-binding protein. We solved the crystal structure of GpsB and the interaction interfaces in both proteins are identified and validated. The inactivation of gpsB results in strongly attenuated virulence in animal experiments, comparable in degree to classical listerial virulence factor mutants. Therefore, GpsB is essential for in vitro and in vivo growth of a highly virulent food-borne pathogen, suggesting that GpsB could be a target for the future design of novel antibacterials.

PubMed: 26575090
DOI: 10.1111/MMI.13279

Experimental method

X-RAY DIFFRACTION (1.6 Å)