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5H7Y

Structure of immunity protein TplEi of T6SS from Pseudomonas aeruginosa complexed with "L" peptide

Summary for 5H7Y
Entry DOI10.2210/pdb5h7y/pdb
Related5H7Z
DescriptorUncharacterized protein (3 entities in total)
Functional Keywordsantimicrobial peptide, effector -immunity complex, inhibitor, hydrolase inhibitor-peptide complex, hydrolase inhibitor/peptide
Biological sourcePseudomonas aeruginosa PAO1
More
Total number of polymer chains2
Total formula weight45419.71
Authors
Gao, X.P.,Mu, Z.X.,Cui, S. (deposition date: 2016-11-21, release date: 2017-10-04, Last modification date: 2024-11-06)
Primary citationGao, X.P.,Mu, Z.X.,Qin, B.,Sun, Y.,Cui, S.
Structure-Based Prototype Peptides Targeting the Pseudomonas aeruginosa Type VI Secretion System Effector as a Novel Antibacterial Strategy
Front Cell Infect Microbiol, 7:411-411, 2017
Cited by
PubMed Abstract: The type VI secretion system (T6SS) secretes numerous toxins for bacteria-bacteria competition. TplE is a newly identified trans-kingdom toxin secreted by the T6SS in , while TplEi neutralizes the toxic effect of TplE to protect bacteria autointoxication. Blocking the interaction of TplE-TplEi could unleash the toxin, causing bacterial cell death. In this study, we applied a crystallographic approach to design a structural-based antimicrobial peptides targeting the interaction of TplE and TplEi. We found that a peptide (designed as "L" peptide based on its shape) derived from TplE can form a crystal complex with TplEi after subtilisin treatment and the crystal structure was solved at 2.2Å. The "L" peptide displays strong binding affinity to TplEi and can release the TplE toxin to induce bacteria death . Our findings suggest that as a toxin activator, the "L" peptide could be a possible drug lead for treating infection. Our findings provide an example that the T6SS effector and immunity protein could be a potential drug target against bacteria infection.
PubMed: 28979890
DOI: 10.3389/fcimb.2017.00411
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.195 Å)
Structure validation

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数据于2024-11-13公开中

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