6GPZ

Cell division regulator GpsB in complex with peptide fragment of L. monocytogenes Penicillin Binding Protein PBPA1

Summary for 6GPZ

• Entry DOI: 10.2210/pdb6gpz/pdb
• Descriptor: Cell cycle protein GpsB, LmPBPA1, ZINC ION, ... (5 entities in total)
• Functional Keywords: bacterial cell division regulator, peptidoglycan synthesis regulator, penicillin binding protein interaction partner, protein-peptide complex, cell cycle
• Biological source: Bacillus subtilis subsp. subtilis str. 168; More
• Total number of polymer chains: 3
• Total formula weight: 17668.68

Authors

Cleverley, R.M.,Lewis, R.J.,Rutter, Z.J. (deposition date: 2018-06-07, release date: 2019-01-23, Last modification date: 2024-01-17)

Primary citation

Cleverley, R.M.,Rutter, Z.J.,Rismondo, J.,Corona, F.,Tsui, H.T.,Alatawi, F.A.,Daniel, R.A.,Halbedel, S.,Massidda, O.,Winkler, M.E.,Lewis, R.J.
The cell cycle regulator GpsB functions as cytosolic adaptor for multiple cell wall enzymes.
Nat Commun, 10:261-261, 2019

PubMed Abstract: Bacterial growth and cell division requires precise spatiotemporal regulation of the synthesis and remodelling of the peptidoglycan layer that surrounds the cytoplasmic membrane. GpsB is a cytosolic protein that affects cell wall synthesis by binding cytoplasmic mini-domains of peptidoglycan synthases to ensure their correct subcellular localisation. Here, we describe critical structural features for the interaction of GpsB with peptidoglycan synthases from three bacterial species (Bacillus subtilis, Listeria monocytogenes and Streptococcus pneumoniae) and suggest their importance for cell wall growth and viability in L. monocytogenes and S. pneumoniae. We use these structural motifs to identify novel partners of GpsB in B. subtilis and extend the members of the GpsB interactome in all three bacterial species. Our results support that GpsB functions as an adaptor protein that mediates the interaction between membrane proteins, scaffolding proteins, signalling proteins and enzymes to generate larger protein complexes at specific sites in a bacterial cell cycle-dependent manner.

PubMed: 30651563
DOI: 10.1038/s41467-018-08056-2

Experimental method

X-RAY DIFFRACTION (1.6 Å)