6SLC

Mutations in SsgB correlate to longitudinal cell division during sporulation of Streptomyces coelicolor

This is a non-PDB format compatible entry.

Summary for 6SLC

• Entry DOI: 10.2210/pdb6slc/pdb
• Related: 6SUJ
• Descriptor: Sporulation and cell division protein SsgA, DI(HYDROXYETHYL)ETHER, GLYCEROL, ... (5 entities in total)
• Functional Keywords: beta barrel, anti-parallel beta-sheet interfaces, cell division component, cell cycle
• Biological source: Streptomyces sp. Ag82_O1-9
• Total number of polymer chains: 3
• Total formula weight: 53182.81

Authors

Xiao, X.S.,Willemse, J. (deposition date: 2019-08-19, release date: 2020-08-26, Last modification date: 2024-01-24)

Primary citation

Xiao, X.,Willemse, J.,Voskamp, P.,Li, X.,Prota, A.E.,Lamers, M.,Pannu, N.,Abrahams, J.P.,van Wezel, G.P.
Ectopic positioning of the cell division plane is associated with single amino acid substitutions in the FtsZ-recruiting SsgB in Streptomyces .
Open Biology, 11:200409-200409, 2021

PubMed Abstract: In most bacteria, cell division begins with the polymerization of the GTPase FtsZ at mid-cell, which recruits the division machinery to initiate cell constriction. In the filamentous bacterium , cell division is positively controlled by SsgB, which recruits FtsZ to the future septum sites and promotes Z-ring formation. Here, we show that various amino acid (aa) substitutions in the highly conserved SsgB protein result in ectopically placed septa that sever spores diagonally or along the long axis, perpendicular to the division plane. Fluorescence microscopy revealed that between 3.3% and 9.8% of the spores of strains expressing SsgB E120 variants were severed ectopically. Biochemical analysis of SsgB variant E120G revealed that its interaction with FtsZ had been maintained. The crystal structure of SsgB was resolved and the key residues were mapped on the structure. Notably, residue substitutions (V115G, G118V, E120G) that are associated with septum misplacement localize in the 2-3 loop region that links the final helix and the rest of the protein. Structural analyses and molecular simulation revealed that these residues are essential for maintaining the proper angle of helix 3. Our data suggest that besides altering FtsZ, aa substitutions in the FtsZ-recruiting protein SsgB also lead to diagonally or longitudinally divided cells in .

PubMed: 33622102
DOI: 10.1098/rsob.200409

Experimental method

X-RAY DIFFRACTION (2.3 Å)