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- EMDB-51308: Cryo-EM Structure of Pentameric Outer Membrane Protein A from Bde... -
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Open data
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Basic information
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Title | Cryo-EM Structure of Pentameric Outer Membrane Protein A from Bdellovibrio bacteriovorus | ||||||||||||
![]() | Overall Map | ||||||||||||
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![]() | Outer membrane protein / porin / beta-barrel / LIPID BINDING PROTEIN | ||||||||||||
Function / homology | Major outer membrane protein![]() | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.85 Å | ||||||||||||
![]() | Parr RJ / Ratkeviciute G / Lovering AL | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: A porin-like protein used by bacterial predators defines a wider lipid-trapping superfamily. Authors: Rebecca J Parr / Yoann G Santin / Giedrė Ratkevičiūte / Simon G Caulton / Paul Radford / Dominik Gurvič / Matthew Jenkins / Matthew T Doyle / Liam Mead / Augustinas Silale / Bert van den ...Authors: Rebecca J Parr / Yoann G Santin / Giedrė Ratkevičiūte / Simon G Caulton / Paul Radford / Dominik Gurvič / Matthew Jenkins / Matthew T Doyle / Liam Mead / Augustinas Silale / Bert van den Berg / Timothy J Knowles / R Elizabeth Sockett / Phillip J Stansfeld / Géraldine Laloux / Andrew L Lovering / ![]() ![]() ![]() Abstract: Outer membrane proteins (OMPs) define the surface biology of Gram-negative bacteria, with roles in adhesion, transport, catalysis and signalling. Specifically, porin beta-barrels are common diffusion ...Outer membrane proteins (OMPs) define the surface biology of Gram-negative bacteria, with roles in adhesion, transport, catalysis and signalling. Specifically, porin beta-barrels are common diffusion channels, predominantly monomeric/trimeric in nature. Here we show that the major OMP of the bacterial predator Bdellovibrio bacteriovorus, PopA, differs from this architecture, forming a pentameric porin-like superstructure. Our X-ray and cryo-EM structures reveal a bowl-shape composite outer β-wall, which houses a central chamber that encloses a section of the lipid bilayer. We demonstrate that PopA, reported to insert into prey inner membrane, causes defects when directed into Escherichia coli membranes. We discover widespread PopA homologues, including likely tetramers and hexamers, that retain the lipid chamber; a similar chamber is formed by an unrelated smaller closed-barrel family, implicating this as a general feature. Our work thus defines oligomeric OMP superfamilies, whose deviation from prior structures requires us to revisit existing membrane-interaction motifs and folding models. | ||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 97.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 18.5 KB 18.5 KB | Display Display | ![]() |
Images | ![]() | 126.5 KB | ||
Masks | ![]() | 103 MB | ![]() | |
Filedesc metadata | ![]() | 6.4 KB | ||
Others | ![]() ![]() | 95.5 MB 95.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 989.7 KB | Display | ![]() |
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Full document | ![]() | 989.2 KB | Display | |
Data in XML | ![]() | 13.2 KB | Display | |
Data in CIF | ![]() | 15.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9gf0MC ![]() 9ga1C 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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Annotation | Overall Map | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.835 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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-Half map: #2
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Density Histograms |
-Half map: #1
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Density Histograms |
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Sample components
-Entire : Pentameric Outer Membrane protein A, PopA
Entire | Name: Pentameric Outer Membrane protein A, PopA |
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Components |
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-Supramolecule #1: Pentameric Outer Membrane protein A, PopA
Supramolecule | Name: Pentameric Outer Membrane protein A, PopA / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Major outer membrane protein
Macromolecule | Name: Major outer membrane protein / type: protein_or_peptide / ID: 1 / Number of copies: 5 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 37.092637 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: SKARVEALAN SRHVLDFQTA FDRPYQFMAL SEQATIEWGN TGDANPHAEG GFVKRHGDDS AFGAYFGRRS ADFSEAVQTV RDASSHHHH HHGSSNPAFA DLMFEQNGLN LFYASKMGEW TWGVTAKYSN GKNEDPTVGT KATSAGVAVA ASNGTWDFEL V QGFTGKSE ...String: SKARVEALAN SRHVLDFQTA FDRPYQFMAL SEQATIEWGN TGDANPHAEG GFVKRHGDDS AFGAYFGRRS ADFSEAVQTV RDASSHHHH HHGSSNPAFA DLMFEQNGLN LFYASKMGEW TWGVTAKYSN GKNEDPTVGT KATSAGVAVA ASNGTWDFEL V QGFTGKSE LDNGTVTAEV ESKGLTNVTV GYHMSPEMEV YGNVKMSKVE ADLNGTPIEV ETTSYKVGMV NTLAKSEEGN FF YGVEVAS TKVKDDSESL LLPVYMGVEH NAASWLVLRA SVAQNVILNE TKDDATGNKT DEDSTRMAAG AGIKFGKSVI DAS FAGSTT GVINANNLFS QVAYTYTF UniProtKB: Major outer membrane protein |
-Macromolecule #2: water
Macromolecule | Name: water / type: ligand / ID: 2 / Number of copies: 33 / Formula: HOH |
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Molecular weight | Theoretical: 18.015 Da |
Chemical component information | ![]() ChemComp-HOH: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 0.02 mg/mL | ||||||||||||
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Buffer | pH: 8 Component:
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Grid | Model: Quantifoil R1.2/1.3 / Material: GRAPHENE OXIDE / Mesh: 200 | ||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV |
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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: 55.4 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 1.2 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Initial model | Chain - Source name: Other / Chain - Initial model type: other / Details: Crystallographic stucture |
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Refinement | Protocol: OTHER |
Output model | ![]() PDB-9gf0: |