期刊
STRUCTURE
卷 22, 期 7, 页码 1047-1054出版社
CELL PRESS
DOI: 10.1016/j.str.2014.04.017
关键词
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资金
- BBSRC [BB/I020012/1]
- EC DIVINOCELL [HEALTH-F3-2009223431]
- EMBO long-term fellowship
- CEA
- FRISBI [ANR-10-INSB-05-02]
- GRAL [ANR-10-LABX-49-01]
- IR-RMN-THC [FR3050 CNRS]
- Biotechnology and Biological Sciences Research Council [BB/I020012/1] Funding Source: researchfish
- BBSRC [BB/I020012/1] Funding Source: UKRI
The bacterial cell envelope contains the stress-bearing peptidoglycan layer, which is enlarged during cell growth and division by membrane-anchored synthases guided by cytoskeletal elements. In Escherichia coli, the major peptidoglycan synthase PBP1A requires stimulation by the outer-membrane-anchored lipoprotein LpoA. Whereas the C-terminal domain of LpoA interacts with PBP1A to stimulate its peptide crosslinking activity, little is known about the role of the N-terminal domain. Herein we report its NMR structure, which adopts an all-alpha-helical fold comprising a series of helix-turn-helix tetratricopeptide-repeat ( TPR)-like motifs. NMR spectroscopy of full-length LpoA revealed two extended flexible regions in the C-terminal domain and limited, if any, flexibility between the N- and C-terminal domains. Analytical ultracentrifugation and small-angle X-ray scattering results are consistent with LpoA adopting an elongated shape, with dimensions sufficient to span from the outer membrane through the periplasm to interact with the peptidoglycan synthase PBP1A.
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