6TIF

ReoM- Listeria monocytogenes

Summary for 6TIF

• Entry DOI: 10.2210/pdb6tif/pdb
• Descriptor: UPF0297 protein lmo1503, SULFATE ION (3 entities in total)
• Functional Keywords: 5-helical bundle, dimer, listeria monocytogenes, phosphoprotein, cell cycle
• Biological source: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
• Total number of polymer chains: 2
• Total formula weight: 21502.22

Authors

Rutter, Z.J.,Lewis, R.J. (deposition date: 2019-11-22, release date: 2020-06-10, Last modification date: 2024-01-24)

Primary citation

Wamp, S.,Rutter, Z.J.,Rismondo, J.,Jennings, C.E.,Moller, L.,Lewis, R.J.,Halbedel, S.
PrkA controls peptidoglycan biosynthesis through the essential phosphorylation of ReoM.
Elife, 9:-, 2020

PubMed Abstract: Peptidoglycan (PG) is the main component of bacterial cell walls and the target for many antibiotics. PG biosynthesis is tightly coordinated with cell wall growth and turnover, and many of these control activities depend upon PASTA-domain containing eukaryotic-like serine/threonine protein kinases (PASTA-eSTK) that sense PG fragments. However, only a few PG biosynthetic enzymes are direct kinase substrates. Here, we identify the conserved ReoM protein as a novel PASTA-eSTK substrate in the Gram-positive pathogen . Our data show that the phosphorylation of ReoM is essential as it controls ClpCP-dependent proteolytic degradation of the essential enzyme MurA, which catalyses the first committed step in PG biosynthesis. We also identify ReoY as a second novel factor required for degradation of ClpCP substrates. Collectively, our data imply that the first committed step of PG biosynthesis is activated through control of ClpCP protease activity in response to signals of PG homeostasis imbalance.

PubMed: 32469310
DOI: 10.7554/eLife.56048

Experimental method

X-RAY DIFFRACTION (1.6 Å)