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- EMDB-33321: Cryo-EM structure of the bacteriocin-receptor-immunity ternary co... -
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Open data
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Basic information
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Title | Cryo-EM structure of the bacteriocin-receptor-immunity ternary complex from Lactobacillus sakei | |||||||||
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![]() | antimicrobial peptides / bacteriocins / pediocin-like/class IIa bacteriocins / antibiotic resistance / mannose phosphotransferase / man-PTS / immunity / self-protection / MEMBRANE PROTEIN / MEMBRANE PROTEIN-IMMUNE SYSTEM complex | |||||||||
Function / homology | ![]() bacteriocin immunity / phosphoenolpyruvate-dependent sugar phosphotransferase system / killing of cells of another organism / defense response to bacterium / extracellular region / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.54 Å | |||||||||
![]() | Wang JW | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural Basis of the Immunity Mechanisms of Pediocin-like Bacteriocins. Authors: Liyan Zhu / Jianwei Zeng / Jiawei Wang / ![]() Abstract: Pediocin-like bacteriocins, also designated class IIa bacteriocins, are ribosomally synthesized antimicrobial peptides targeting species closely related to the producers. They act on the cytoplasmic ...Pediocin-like bacteriocins, also designated class IIa bacteriocins, are ribosomally synthesized antimicrobial peptides targeting species closely related to the producers. They act on the cytoplasmic membrane of Gram-positive cells by dissipating the transmembrane electrical potential through pore formation with the mannose phosphotransferase system (man-PTS) as the target/receptor. Bacteriocin-producing strains also synthesize a cognate immunity protein that protects them against their own bacteriocins. Herein, we report the cryo-electron microscopy structure of the bacteriocin-receptor-immunity ternary complex from Lactobacillus sakei. The complex structure reveals that pediocin-like bacteriocins bind to the same position on the Core domain of man-PTS, while the C-terminal helical tails of bacteriocins delimit the opening range of the Core domain away from the Vmotif domain to facilitate transmembrane pore formation. Upon attack of bacteriocins from the extracellular side, man-PTS exposes its cytosolic side for recognition of the N-terminal four-helix bundle of the immunity protein. The C-terminal loop of the immunity protein then inserts into the pore and blocks leakage induced by bacteriocins. Elucidation of the toxicity and immunity mechanisms of pediocin-like bacteriocins could support the design of novel bacteriocins against antibiotic-resistant pathogenic bacteria. Pediocin-like bacteriocins, ribosomally synthesized antimicrobial peptides, are generally co-expressed with cognate immunity proteins to protect the bacteriocin-producing strain from its own bacteriocin. Bacteriocins are considered potential alternatives to conventional antibiotics in the context of the bacterial resistance crisis, but the immunity mechanism is unclear. This study uncovered the mechanisms of action and immunity of class IIa bacteriocins. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 117.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.5 KB 17.5 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 11.3 KB | Display | ![]() |
Images | ![]() | 35 KB | ||
Filedesc metadata | ![]() | 5.8 KB | ||
Others | ![]() ![]() | 115.8 MB 115.8 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7xnoMC ![]() 7xtgC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.8433 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: Half map 1
File | emd_33321_half_map_1.map | ||||||||||||
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Annotation | Half map 1 | ||||||||||||
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Density Histograms |
-Half map: Half map 2
File | emd_33321_half_map_2.map | ||||||||||||
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Annotation | Half map 2 | ||||||||||||
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Density Histograms |
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Sample components
-Entire : The bacteriocin-receptor-immunity ternary complex from Lactobacil...
Entire | Name: The bacteriocin-receptor-immunity ternary complex from Lactobacillus sakei |
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Components |
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-Supramolecule #1: The bacteriocin-receptor-immunity ternary complex from Lactobacil...
Supramolecule | Name: The bacteriocin-receptor-immunity ternary complex from Lactobacillus sakei type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Bacteriocin sakacin-A
Macromolecule | Name: Bacteriocin sakacin-A / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 4.312893 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: ARSYGNGVYC NNKKCWVNRG EATQSIIGGM ISGWASGLAG M UniProtKB: Bacteriocin sakacin-A |
-Macromolecule #2: Mannose permease IIC component
Macromolecule | Name: Mannose permease IIC component / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 27.467719 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MDLNFIQVIL VIFVAFLAGV EGILDQFHFH QPVIACTLIG LVTGNLLPCL ILGGTLQMIA LGWANVGAAV APDAALASIA SAIILVLGG QGKAGVTSAI AIAVPLAVAG LLLTIIVRTL ATGIVHIMDA AAKEGNFRKI EMWQYIAIIM QGVRIAIPAG L ILAIGAGP ...String: MDLNFIQVIL VIFVAFLAGV EGILDQFHFH QPVIACTLIG LVTGNLLPCL ILGGTLQMIA LGWANVGAAV APDAALASIA SAIILVLGG QGKAGVTSAI AIAVPLAVAG LLLTIIVRTL ATGIVHIMDA AAKEGNFRKI EMWQYIAIIM QGVRIAIPAG L ILAIGAGP VKEMLTAMPV WLTDGLAIGG GMVVAVGYAM VINMMATKEV WPFFAIGFVL ATISQLTLIG LGAIGISLAL IY LALSKQG SGNNGGGSNT GDPLGDIIDN Y UniProtKB: Mannose permease IIC component |
-Macromolecule #3: Mannose permease IID component
Macromolecule | Name: Mannose permease IID component / type: protein_or_peptide / ID: 3 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 33.332105 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MAEQLKLTKK DRISVWLRST FLQGSWNYER MQNGGWAYTL IPALKKLYKT KEDRSAALVR HMEFFNTHPY VAAPILGVTL ALEEERANG APIDDVTIQG VKVGMMGPLA GIGDPVFWFT VKPIIGALAA SLAMSGNILG PIIYFVAWNA IRMAFTWYTQ E FGYRAGSK ...String: MAEQLKLTKK DRISVWLRST FLQGSWNYER MQNGGWAYTL IPALKKLYKT KEDRSAALVR HMEFFNTHPY VAAPILGVTL ALEEERANG APIDDVTIQG VKVGMMGPLA GIGDPVFWFT VKPIIGALAA SLAMSGNILG PIIYFVAWNA IRMAFTWYTQ E FGYRAGSK ITEDLSGGIL QDITKGASIL GMFILGSLVN RWVSVKFTPT VSSVKLDKGA FIDWDKLPSG AKGIQSALQQ QA QGLSLTD HKITTLQDNL DSLIPGLAAL GLTLFCMWLL KKKVSPIVII LGLFVVGIVF HLLHLM UniProtKB: Mannose permease IID component |
-Macromolecule #4: Sakacin-A immunity factor
Macromolecule | Name: Sakacin-A immunity factor / type: protein_or_peptide / ID: 4 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 13.747889 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MKHHHHHHHG AAGTSLYKKA GENLYFQGSM KADYKKINSI LTYTSTALKN PKIIKDKDLV VLLTIIQEEA KQNRIFYDYK RKFRPAVTR FTIDNNFEIP DCLVKLLSAV ETPKAWSGFS UniProtKB: Sakacin-A immunity factor |
-Macromolecule #5: alpha-D-mannopyranose
Macromolecule | Name: alpha-D-mannopyranose / type: ligand / ID: 5 / Number of copies: 3 / Formula: MAN |
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Molecular weight | Theoretical: 180.156 Da |
Chemical component information | ![]() ChemComp-MAN: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: NITROGEN |
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Electron microscopy
Microscope | FEI TITAN |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm |