Structure-function analysis of the LytM domain of EnvC, an activator of cell wall remodelling at the Escherichia coli division site
| Autor: | Peters, Nick T, Morlot, Cécile, Yang, Desirée C, Uehara, Tsuyoshi, Vernet, Thierry, Bernhardt, Thomas G |
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| Přispěvatelé: | Department of Microbiology and Immunobiology, Harvard Medical School [Boston] (HMS), 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), Thomas, Frank, 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) |
| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Models
Molecular MESH: Amidohydrolases [SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] Protein Conformation DNA Mutational Analysis Molecular Sequence Data MESH: Sequence Alignment MESH: Catalytic Domain MESH: Escherichia coli Proteins MESH: Amino Acid Sequence Crystallography X-Ray Article Amidohydrolases MESH: Protein Conformation Catalytic Domain Endopeptidases Escherichia coli Amino Acid Sequence MESH: DNA Mutational Analysis MESH: Endopeptidases MESH: Molecular Sequence Data [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] MESH: Escherichia coli Escherichia coli Proteins MESH: Crystallography X-Ray Sequence Alignment MESH: Models Molecular |
| Zdroj: | Molecular Microbiology Molecular Microbiology, 2013, 89 (4), pp.690-701 Molecular Microbiology, Wiley, 2013, 89 (4), pp.690-701 |
| ISSN: | 0950-382X 1365-2958 |
| Popis: | International audience; Proteins with LytM (Peptidase_M23) domains are broadly distributed in bacteria and have been implicated in a variety of important processes, including cell division and cell-shape determination. Most LytM-like proteins that have been structurally and/or biochemically characterized are metallo-endopeptidases that cleave cross-links in the peptidoglycan (PG) cell wall matrix. Notable exceptions are the Escherichia coli cell division proteins EnvC and NlpD. These LytM factors are not hydrolases themselves, but instead serve as activators that stimulate PG cleavage by target enzymes called amidases to promote cell separation. Here we report the structure of the LytM domain from EnvC, the first structure of a LytM factor implicated in the regulation of PG hydrolysis. As expected, the fold is highly similar to that of other LytM proteins. However, consistent with its role as a regulator, the active-site region is degenerate and lacks a catalytic metal ion. Importantly, genetic analysis indicates that residues in and around this degenerate active site are critical for amidase activation in vivo and in vitro. Thus, in the regulatory LytM factors, the apparent substrate binding pocket conserved in active metallo-endopeptidases has been adapted to control PG hydrolysis by another set of enzymes. |
| Databáze: | OpenAIRE |
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