8i2e | pdb_00008i2e
Crystal structure of Bacillus subtilis LytE in complex with IseA
Structural highlights
FunctionLYTE_BACSU Cell wall hydrolase that cleaves gamma-D-glutamate-meso-diaminopimelate bonds in peptidoglycan (By similarity). Seems to play a role in cell separation during vegetative growth.[1] [2] Publication Abstract from PubMedPeptidoglycan, 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 peptidoglycan 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. Structural insights into the regulation of peptidoglycan DL-endopeptidases by inhibitory protein IseA.,Tandukar S, Kwon E, Kim DY Structure. 2023 Mar 11:S0969-2126(23)00075-8. doi: 10.1016/j.str.2023.02.013. PMID:36963396[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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