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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Molecular architecture of the PBP2-MreC core bacterial cell wall synthesis complex

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Autor(es):
Contreras-Martel, Carlos [1] ; Martins, Alexandre [1] ; Ecobichon, Chantal [2, 3] ; Trindade, Daniel Maragno [4] ; Mattei, Pierre-Jean [1] ; Hicham, Samia [2, 3] ; Hardouin, Pierre [1] ; El Ghachi, Meriem [2, 3] ; Boneca, Ivo G. [2, 3] ; Dessen, Andrea [1, 4]
Número total de Autores: 10
Afiliação do(s) autor(es):
[1] Univ Grenoble Alpes, CNRS, CEA, IBS, Bacterial Pathogenesis Grp, F-38000 Grenoble - France
[2] Inst Pasteur, Unit Biol & Genet Bacterial Cell Wall, F-75015 Paris - France
[3] INSERM, Grp Avenir, F-75015 Paris - France
[4] CNPEM, Brazilian Biosci Natl Lab LNBio, BR-13084971 Campinas, SP - Brazil
Número total de Afiliações: 4
Tipo de documento: Artigo Científico
Fonte: NATURE COMMUNICATIONS; v. 8, OCT 3 2017.
Citações Web of Science: 9
Resumo

Bacterial cell wall biosynthesis is an essential process that requires the coordinated activity of peptidoglycan biosynthesis enzymes within multi-protein complexes involved in cell division (the ``divisome{''}) and lateral wall growth (the ``elongasome{''}). MreC is a structural protein that serves as a platform during wall elongation, scaffolding other essential peptidoglycan biosynthesis macromolecules, such as penicillin-binding proteins. Despite the importance of these multi-partite complexes, details of their architecture have remained elusive due to the transitory nature of their interactions. Here, we present the crystal structures of the soluble PBP2: MreC core elongasome complex from Helicobacter pylori, and of uncomplexed PBP2. PBP2 recognizes the two-winged MreC molecule upon opening of its N-terminal region, revealing a hydrophobic zipper that serves as binding platform. The PBP2: MreC interface is essential both for protein recognition in vitro and maintenance of bacterial shape and growth. This work allows visualization as to how peptidoglycan machinery proteins are scaffolded, revealing interaction regions that could be targeted by tailored inhibitors. (AU)

Processo FAPESP: 11/52067-6 - Estruturação de complexos macromoleculares da parede bacteriana: biossíntese e virulência
Beneficiário:Andrea Dessen de Souza e Silva
Linha de fomento: Auxílio à Pesquisa - Programa SPEC