Backbone and side-chain (1)H, (13)C, and (15)N NMR assignments of the N-terminal domain of Escherichia coli LpoA
| Autor: | Adeline Derouaux, Jean-Pierre Simorre, Waldemar Vollmer, Catherine M. Bougault, Gilles Callens, Nicolas L. Jean |
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| Přispěvatelé: | Institut de biologie structurale (IBS - UMR 5075 ), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Centre for Bacterial Cell Biology, Newcastle University [Newcastle], TGIR-RMN-THC FR3050 CNRS, UMS 3518 CNRS-CEA-UJF-EMBL, European Project: 223431,EC:FP7:HEALTH,FP7-HEALTH-2007-B,DIVINOCELL(2009), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Thomas, Frank, Exploiting Gram-negative cell division targets in the test tube to obtain anti-microbial compounds - DIVINOCELL - - EC:FP7:HEALTH2009-03-01 - 2013-08-31 - 223431 - VALID |
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Lipoproteins
[SDV]Life Sciences [q-bio] Cell Molecular Sequence Data Biology medicine.disease_cause Biochemistry Bacterial cell structure 03 medical and health sciences chemistry.chemical_compound Structural Biology medicine Side chain Escherichia coli Amino Acid Sequence Cytoskeleton Nuclear Magnetic Resonance Biomolecular 030304 developmental biology 0303 health sciences Lipid II 030306 microbiology Escherichia coli Proteins Protein Structure Tertiary [SDV] Life Sciences [q-bio] medicine.anatomical_structure chemistry Peptidoglycan Function (biology) Bacterial Outer Membrane Proteins |
| Zdroj: | Biomolecular NMR Assignments Biomolecular NMR Assignments, 2015, pp.11 Biomolecular NMR Assignments, Springer, 2015, pp.11 |
| ISSN: | 1874-270X |
| Popis: | International audience; The peptidoglycan is a major component of the bacterial cell wall and is essential to maintain cellular integrity and cell shape. Penicillin-Binding Proteins (PBPs) catalyze the final biosynthetic steps of peptidoglycan synthesis from lipid II precursor and are the main targets of β-lactam antibiotics. The molecular details of peptidoglycan growth and its regulation are poorly understood. Presumably, PBPs are active in peptidoglycan synthesizing multi-enzyme complexes that are controlled from inside the cell by cytoskeletal elements. Recently, two outer-membrane lipoproteins, LpoA and LpoB, were shown to be required in Escherichia coli for the function of the main peptidoglycan synthases, PBP1A and PBP1B, by stimulating their transpeptidase activity. However, the mechanism of PBP-activation by Lpo proteins is not known, and the Lpo proteins await structural characterization at atomic resolution. Here we present the backbone and side-chain (1)H, (13)C, (15)N NMR assignments of the N-terminal domain of LpoA from E. coli for structural and functional studies. |
| Databáze: | OpenAIRE |
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