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Structural insights into the regulation of peptidoglycan DL-endopeptidases by inhibitory protein IseA

Authors
Tandukar, SudarshanKwon, EunjuKim, Dong Young
Issue Date
May-2023
Publisher
CELL PRESS
Citation
STRUCTURE, v.31, no.5, pp 619 - +
Indexed
SCIE
SCOPUS
Journal Title
STRUCTURE
Volume
31
Number
5
Start Page
619
End Page
+
URI
https://scholarworks.gnu.ac.kr/handle/sw.gnu/68704
DOI
10.1016/j.str.2023.02.013
ISSN
0969-2126
1878-4186
Abstract
Peptidoglycan, a physical barrier that protects bacteria from the environment, is constantly degraded and resynthesized for remodeling during cell growth and division. Because excessive or insufficient peptido-glycan hydrolysis affects bacterial homeostasis and viability, peptidoglycan degradation must be precisely regulated. In Bacillus subtilis, DL-endopeptidases play an essential role in peptidoglycan remodeling, and their activity is regulated by IseA. Here, we report the crystal structure of peptidoglycan DL-endopeptidase LytE complexed with IseA. In the crystal structure, the inhibitory loop connecting the two lobes of IseA blocks the active site of LytE by mimicking its substrate. Consistently, mutations in the inhibitory loop resulted in the loss of IseA activity. The structure also shows that conformational rearrangements in both LytE and IseA restrict access of the inhibitory loop to the LytE catalytic site. These results reveal an inhibition mechanism of peptidoglycan DL-endopeptidase in which the inhibitory protein mimics the substrate but is not degraded.
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자연과학대학 > Division of Life Sciences > Journal Articles

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