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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-32030 | |||||||||
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| Title | Cryo-EM structures of Listeria monocytogenes man-PTS | |||||||||
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Keywords | antimicrobial peptides / bacteriocins / pediocin PA-1 / pediocin-like/class IIa bacteriocins / antibiotic resistance / mannose phosphotransferase / man-PTS / MEMBRANE PROTEIN | |||||||||
| Function / homology | Function and homology informationphosphoenolpyruvate-dependent sugar phosphotransferase system / plasma membrane Similarity search - Function | |||||||||
| Biological species | Listeria monocytogenes (bacteria) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.12 Å | |||||||||
Authors | Wang JW | |||||||||
| Funding support | China, 2 items
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Citation | Journal: Appl Environ Microbiol / Year: 2022Title: Structural Basis of Pore Formation in the Mannose Phosphotransferase System by Pediocin PA-1. Authors: Liyan Zhu / Jianwei Zeng / Chang Wang / Jiawei Wang / ![]() Abstract: Bacteriocins are ribosomally synthesized bacterial antimicrobial peptides that have a narrow spectrum of antibacterial activity against species closely related to the producers. Pediocin-like (or ...Bacteriocins are ribosomally synthesized bacterial antimicrobial peptides that have a narrow spectrum of antibacterial activity against species closely related to the producers. Pediocin-like (or class IIa) bacteriocins (PLBs) exhibit antibacterial activity against several Gram-positive bacterial strains by forming pores in the cytoplasmic membrane of target cells with a specific receptor, the mannose phosphotransferase system (man-PTS). In this study, we report the cryo-electron microscopy structures of man-PTS from Listeria monocytogenes alone and its complex with pediocin PA-1, the first and most extensively studied representative PLB, at resolutions of 3.12 and 2.45 Å, respectively. The structures revealed that the binding of pediocin PA-1 opens the Core domain of man-PTS away from its Vmotif domain, creating a pore through the cytoplasmic membranes of target cells. During this process, the N-terminal β-sheet region of pediocin PA-1 can specifically attach to the extracellular surface of the man-PTS Core domain, whereas the C-terminal half penetrates the membrane and cracks the man-PTS like a wedge. Thus, our findings shed light on a design of novel PLBs that can kill the target pathogenic bacteria. Listeria monocytogenes is a ubiquitous microorganism responsible for listeriosis, a rare but severe disease in humans, who become infected by ingesting contaminated food products (i.e., dairy, meat, fish, and vegetables): the disease has a fatality rate of 33%. Pediocin PA-1 is an important commercial additive used in food production to inhibit species. The mannose phosphotransferase system (man-PTS) is responsible for the sensitivity of Listeria monocytogenes to pediocin PA-1. In this study, we report the cryo-EM structures of man-PTS from Listeria monocytogenes alone and its complex with pediocin PA-1 at resolutions of 3.12 and 2.45 Å, respectively. Our results facilitate the understanding of the mode of action of class IIa bacteriocins as an alternative to antibiotics. | |||||||||
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Structure visualization
| Movie |
Movie viewer |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
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Downloads & links
-EMDB archive
| Map data | emd_32030.map.gz | 4.6 MB | EMDB map data format | |
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| Header (meta data) | emd-32030-v30.xml emd-32030.xml | 15.3 KB 15.3 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_32030_fsc.xml | 9.1 KB | Display | FSC data file |
| Images | emd_32030.png | 144.8 KB | ||
| Filedesc metadata | emd-32030.cif.gz | 6.9 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-32030 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-32030 | HTTPS FTP |
-Validation report
| Summary document | emd_32030_validation.pdf.gz | 383.1 KB | Display | EMDB validaton report |
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| Full document | emd_32030_full_validation.pdf.gz | 382.6 KB | Display | |
| Data in XML | emd_32030_validation.xml.gz | 10.7 KB | Display | |
| Data in CIF | emd_32030_validation.cif.gz | 14.1 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-32030 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-32030 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 7vlxMC ![]() 7vlyC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_32030.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.0742 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : mannose-specific PTS system from Listeria monocytogenes
| Entire | Name: mannose-specific PTS system from Listeria monocytogenes |
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| Components |
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-Supramolecule #1: mannose-specific PTS system from Listeria monocytogenes
| Supramolecule | Name: mannose-specific PTS system from Listeria monocytogenes type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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| Source (natural) | Organism: Listeria monocytogenes (bacteria) |
-Macromolecule #1: Mannose/fructose/sorbose family PTS transporter subunit IIC
| Macromolecule | Name: Mannose/fructose/sorbose family PTS transporter subunit IIC type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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| Source (natural) | Organism: Listeria monocytogenes (bacteria) |
| Molecular weight | Theoretical: 27.377561 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MSVISIILVV LIAFLAGIEG ILDEFQFHQP LIACTLIGLV TGNLTACIIL GGTLQMIALG WANIGAAVAP DAALASVASA IILVLGGQG VAGIPSAIAI AIPLAVAGLF LTMIVRTLAV PIVHLMDRAA EKGNIRSVEW LHISAICMQG IRIAIPAAAL L FIPADSVQ ...String: MSVISIILVV LIAFLAGIEG ILDEFQFHQP LIACTLIGLV TGNLTACIIL GGTLQMIALG WANIGAAVAP DAALASVASA IILVLGGQG VAGIPSAIAI AIPLAVAGLF LTMIVRTLAV PIVHLMDRAA EKGNIRSVEW LHISAICMQG IRIAIPAAAL L FIPADSVQ SFLEAMPAWL TDGMAIGGGM VVAVGYALVI NMMATKEVWP FFVIGFVVAA ISQLTLIAIG ALGVALALIY LN LSKMGGG NSNGGGGGNS RDPLGDILND Y UniProtKB: Mannose/fructose/sorbose family PTS transporter subunit IIC |
-Macromolecule #2: PTS mannose family transporter subunit IID
| Macromolecule | Name: PTS mannose family transporter subunit IID / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO |
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| Source (natural) | Organism: Listeria monocytogenes (bacteria) |
| Molecular weight | Theoretical: 33.402164 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MAEKIELSKR DRLRVAWRST FIQGSWNYER MQNGGWAFSM IPAIKKLYKT KEDRSSALKR HLEFFNTHPY IASPILGVTL ALEEERANG AEVDDVAIQG VKVGMMGPLA GVGDPVFWFT IRPMLGALGA SLALSGNILG PILFFVAWNV IRWGFMWYTQ E FGYKAGSK ...String: MAEKIELSKR DRLRVAWRST FIQGSWNYER MQNGGWAFSM IPAIKKLYKT KEDRSSALKR HLEFFNTHPY IASPILGVTL ALEEERANG AEVDDVAIQG VKVGMMGPLA GVGDPVFWFT IRPMLGALGA SLALSGNILG PILFFVAWNV IRWGFMWYTQ E FGYKAGSK ITDDLSGGLL QDITKGASIL GMFVLAALVQ RWVNIQFAPI ISKVKLDEGA YIDWSHLPQG AQGIKTALQQ QQ AGLALSE IKVTTLQNNL DNLIPGLAAV ALTFLCMWLL KKKISPIIII LGLFVVGIVG HLIGLL UniProtKB: PTS mannose family transporter subunit IID |
-Macromolecule #3: alpha-D-mannopyranose
| Macromolecule | Name: alpha-D-mannopyranose / type: ligand / ID: 3 / 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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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.4 |
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| Vitrification | Cryogen name: NITROGEN |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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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: LAB6 |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
Listeria monocytogenes (bacteria)
Authors
China, 2 items
Citation
UCSF Chimera










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