6TIF
ReoM- Listeria monocytogenes
6TIF の概要
| エントリーDOI | 10.2210/pdb6tif/pdb |
| 分子名称 | UPF0297 protein lmo1503, SULFATE ION (3 entities in total) |
| 機能のキーワード | 5-helical bundle, dimer, listeria monocytogenes, phosphoprotein, cell cycle |
| 由来する生物種 | Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 21502.22 |
| 構造登録者 | |
| 主引用文献 | 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 Cited by 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: 32469310DOI: 10.7554/eLife.56048 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.6 Å) |
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