8BVE
MoeA2 from Corynebacterium glutamicum
Summary for 8BVE
| Entry DOI | 10.2210/pdb8bve/pdb |
| Descriptor | Molybdopterin molybdenumtransferase, SODIUM ION, CITRIC ACID, ... (4 entities in total) |
| Functional Keywords | molybdopterin molybdotransferase; cell division; gephyrin-like protein; corynebacteriales, cell cycle |
| Biological source | Corynebacterium glutamicum ATCC 13032 |
| Total number of polymer chains | 2 |
| Total formula weight | 88697.75 |
| Authors | Martinez, M.,Haouz, A.,Wehenkel, A.M.,Alzari, P.M. (deposition date: 2022-12-03, release date: 2023-02-22, Last modification date: 2024-10-23) |
| Primary citation | Martinez, M.,Petit, J.,Leyva, A.,Sogues, A.,Megrian, D.,Rodriguez, A.,Gaday, Q.,Ben Assaya, M.,Portela, M.M.,Haouz, A.,Ducret, A.,Grangeasse, C.,Alzari, P.M.,Duran, R.,Wehenkel, A.M. Eukaryotic-like gephyrin and cognate membrane receptor coordinate corynebacterial cell division and polar elongation. Nat Microbiol, 8:1896-1910, 2023 Cited by PubMed Abstract: The order Corynebacteriales includes major industrial and pathogenic Actinobacteria such as Corynebacterium glutamicum or Mycobacterium tuberculosis. These bacteria have multi-layered cell walls composed of the mycolyl-arabinogalactan-peptidoglycan complex and a polar growth mode, thus requiring tight coordination between the septal divisome, organized around the tubulin-like protein FtsZ, and the polar elongasome, assembled around the coiled-coil protein Wag31. Here, using C. glutamicum, we report the discovery of two divisome members: a gephyrin-like repurposed molybdotransferase (Glp) and its membrane receptor (GlpR). Our results show how cell cycle progression requires interplay between Glp/GlpR, FtsZ and Wag31, showcasing a crucial crosstalk between the divisome and elongasome machineries that might be targeted for anti-mycobacterial drug discovery. Further, our work reveals that Corynebacteriales have evolved a protein scaffold to control cell division and morphogenesis, similar to the gephyrin/GlyR system that mediates synaptic signalling in higher eukaryotes through network organization of membrane receptors and the microtubule cytoskeleton. PubMed: 37679597DOI: 10.1038/s41564-023-01473-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.14 Å) |
Structure validation
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