6PL6

Structural coordination of polymerization and crosslinking by a peptidoglycan synthase complex

Summary for 6PL6

• Entry DOI: 10.2210/pdb6pl6/pdb
• Related: 6PL5
• Descriptor: Peptidoglycan glycosyltransferase RodA, Penicillin-binding protein 2/cell division protein FtsI, Unknown peptide, ... (4 entities in total)
• Functional Keywords: peptidoglycan glycosyltransferase, transmembrane protein, shape elongation division and sporulation, elongasome, peptidoglycan transpeptidase, membrane protein
• Biological source: Thermus thermophilus HB8; More
• Total number of polymer chains: 3
• Total formula weight: 107311.51

Authors

Sjodt, M.,Rohs, P.D.A.,Erlandson, S.C.,Zheng, S.,Rudner, D.Z.,Bernhardt, T.G.,Kruse, A.C. (deposition date: 2019-06-30, release date: 2020-03-18, Last modification date: 2024-11-20)

Primary citation

Sjodt, M.,Rohs, P.D.A.,Gilman, M.S.A.,Erlandson, S.C.,Zheng, S.,Green, A.G.,Brock, K.P.,Taguchi, A.,Kahne, D.,Walker, S.,Marks, D.S.,Rudner, D.Z.,Bernhardt, T.G.,Kruse, A.C.
Structural coordination of polymerization and crosslinking by a SEDS-bPBP peptidoglycan synthase complex.
Nat Microbiol, 5:813-820, 2020

PubMed Abstract: The shape, elongation, division and sporulation (SEDS) proteins are a highly conserved family of transmembrane glycosyltransferases that work in concert with class B penicillin-binding proteins (bPBPs) to build the bacterial peptidoglycan cell wall. How these proteins coordinate polymerization of new glycan strands with their crosslinking to the existing peptidoglycan meshwork is unclear. Here, we report the crystal structure of the prototypical SEDS protein RodA from Thermus thermophilus in complex with its cognate bPBP at 3.3 Å resolution. The structure reveals a 1:1 stoichiometric complex with two extensive interaction interfaces between the proteins: one in the membrane plane and the other at the extracytoplasmic surface. When in complex with a bPBP, RodA shows an approximately 10 Å shift of transmembrane helix 7 that exposes a large membrane-accessible cavity. Negative-stain electron microscopy reveals that the complex can adopt a variety of different conformations. These data define the bPBP pedestal domain as the key allosteric activator of RodA both in vitro and in vivo, explaining how a SEDS-bPBP complex can coordinate its dual enzymatic activities of peptidoglycan polymerization and crosslinking to build the cell wall.

PubMed: 32152588
DOI: 10.1038/s41564-020-0687-z

Experimental method

X-RAY DIFFRACTION (3.3 Å)