[English] 日本語
Yorodumi- EMDB-44164: Pseudomonas phage Pa193 Neck (portal and head-to-tail proteins) -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-44164 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Pseudomonas phage Pa193 Neck (portal and head-to-tail proteins) | |||||||||
Map data | ||||||||||
Sample |
| |||||||||
Keywords | phage / bacteriophage / gene product (gp19) / STRUCTURAL PROTEIN / VIRAL PROTEIN / gene product 28 (gp28) / head-to-tail protein / portal protein | |||||||||
Function / homology | Protein of unknown function DUF4054 / Inorganic pyrophosphatase domain / Protein of unknown function (DUF4054) / Inorganic Pyrophosphatase / Protein of unknown function DUF1073 / Phage portal protein / Phage protein / Inorganic pyrophosphatase domain-containing protein Function and homology information | |||||||||
Biological species | Pseudomonas virus Pa193 | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.2 Å | |||||||||
Authors | Iglesias SM / Cingolani G | |||||||||
Funding support | United States, 1 items
| |||||||||
Citation | Journal: Commun Biol / Year: 2024 Title: Cryo-EM analysis of Pseudomonas phage Pa193 structural components. Authors: Stephano M Iglesias / Chun-Feng David Hou / Johnny Reid / Evan Schauer / Renae Geier / Angela Soriaga / Lucy Sim / Lucy Gao / Julian Whitelegge / Pierre Kyme / Deborah Birx / Sebastien Lemire / Gino Cingolani / Abstract: The World Health Organization has designated Pseudomonas aeruginosa as a critical pathogen for the development of new antimicrobials. Bacterial viruses, or bacteriophages, have been used in various ...The World Health Organization has designated Pseudomonas aeruginosa as a critical pathogen for the development of new antimicrobials. Bacterial viruses, or bacteriophages, have been used in various clinical settings, commonly called phage therapy, to address this growing public health crisis. Here, we describe a high-resolution structural atlas of a therapeutic, contractile-tailed Pseudomonas phage, Pa193. We used bioinformatics, proteomics, and cryogenic electron microscopy single particle analysis to identify, annotate, and build atomic models for 21 distinct structural polypeptide chains forming the icosahedral capsid, neck, contractile tail, and baseplate. We identified a putative scaffolding protein stabilizing the interior of the capsid 5-fold vertex. We also visualized a large portion of Pa193 ~ 500 Å long tail fibers and resolved the interface between the baseplate and tail fibers. The work presented here provides a framework to support a better understanding of phages as biomedicines for phage therapy and inform engineering opportunities. | |||||||||
History |
|
-Structure visualization
Supplemental images |
---|
-Downloads & links
-EMDB archive
Map data | emd_44164.map.gz | 64.7 MB | EMDB map data format | |
---|---|---|---|---|
Header (meta data) | emd-44164-v30.xml emd-44164.xml | 20 KB 20 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_44164_fsc.xml | 11.3 KB | Display | FSC data file |
Images | emd_44164.png | 17.6 KB | ||
Masks | emd_44164_msk_1.map | 125 MB | Mask map | |
Filedesc metadata | emd-44164.cif.gz | 6.1 KB | ||
Others | emd_44164_additional_1.map.gz emd_44164_half_map_1.map.gz emd_44164_half_map_2.map.gz | 112.4 MB 92.1 MB 91.9 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-44164 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-44164 | HTTPS FTP |
-Validation report
Summary document | emd_44164_validation.pdf.gz | 818.3 KB | Display | EMDB validaton report |
---|---|---|---|---|
Full document | emd_44164_full_validation.pdf.gz | 817.8 KB | Display | |
Data in XML | emd_44164_validation.xml.gz | 19.2 KB | Display | |
Data in CIF | emd_44164_validation.cif.gz | 25 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-44164 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-44164 | HTTPS FTP |
-Related structure data
Related structure data | 9b41MC 9b40C 9b42C 9b45C M: atomic model generated by this map C: citing same article (ref.) |
---|---|
Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
---|
-Map
File | Download / File: emd_44164.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.34 Å | ||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-Mask #1
File | emd_44164_msk_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Additional map: #1
File | emd_44164_additional_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: #2
File | emd_44164_half_map_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: #1
File | emd_44164_half_map_2.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Sample components
-Entire : Pseudomonas virus Pa193
Entire | Name: Pseudomonas virus Pa193 |
---|---|
Components |
|
-Supramolecule #1: Pseudomonas virus Pa193
Supramolecule | Name: Pseudomonas virus Pa193 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 2590837 / Sci species name: Pseudomonas virus Pa193 / Virus type: VIRION / Virus isolate: OTHER / Virus enveloped: No / Virus empty: No |
---|
-Macromolecule #1: gp19 Portal
Macromolecule | Name: gp19 Portal / type: protein_or_peptide / ID: 1 / Number of copies: 12 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: Pseudomonas virus Pa193 |
Molecular weight | Theoretical: 84.4785 KDa |
Sequence | String: MFKLSWIFGR KKDNAACSES APEKVAQIPQ HDPLDPMIKL GRIRGWNVEP EKAPVIRSVK DFLEPGLSVA MDSAYGDGPT PAAKAAAGG QNPYVVPTML QDWYNSQGFI GYQACAIISQ HWLVDKACSM SGEDAARNGW ELKSDGRKLS DEQSALIARR D MEFRVKDN ...String: MFKLSWIFGR KKDNAACSES APEKVAQIPQ HDPLDPMIKL GRIRGWNVEP EKAPVIRSVK DFLEPGLSVA MDSAYGDGPT PAAKAAAGG QNPYVVPTML QDWYNSQGFI GYQACAIISQ HWLVDKACSM SGEDAARNGW ELKSDGRKLS DEQSALIARR D MEFRVKDN LVELNRFKNV FGVRIALFVV ESDDPDYYEK PFNPDGITPG SYKGISQIDP YWAMPQLTAG STADPSSEHF YE PDFWIIS GKKYHRSHLV VVRGPQPPDI LKPTYIFGGI PLTQRIYERV YAAERTANEA PLLAMSKRTS TIHVDVEKAI ANE DAFNAR LAFWIANRDN HGVKVLGTDE SMEQFDTNLA DFDSIIMNQY QLVAAIAKTP ATKLLGTSPK GFNATGEHET ISYH EELES IQEHIFDPLL ERHYLLLAKS EEIDVQLEIV WNPVDSTSSQ QQAELNNKKA ATDEIYINSG VVSPDEVRER LRDDP RSGY NRLTDDQAET EPGMSPENLA EFEKAGAQSA KAKGEAERAE AQAGAVEGAG DPVPAAPRGT KPLAKAAEEG ASEAAE PPS RPDPKAELRN LLVDLLSKLQ DLDDIKAPDG VDIEHNDAPG VKRTSKPGVS GMEPSVFSSN RIVGPRDHSE LQRIKVN GI TTLIENPRGS IRQGKDGSWR VQMKHHYGFI KGTKGADGDE VDCFVGPNLG SKRVFVVNQV NKEGQFDEHK CMLGFNNI N DAKSGYLSCF RPGWDGLGSI HEVDLPAFRR WLANGDTTKP FGGE UniProtKB: Inorganic pyrophosphatase domain-containing protein |
-Macromolecule #2: gp28 Head-to-tail protein
Macromolecule | Name: gp28 Head-to-tail protein / type: protein_or_peptide / ID: 2 / Number of copies: 12 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: Pseudomonas virus Pa193 |
Molecular weight | Theoretical: 16.885285 KDa |
Sequence | String: MVIFDEHKFR TLFPEFADPA AYPDVRLQMY FDIACEFISD RDSPYRILNG KALEACLYLL TAHLLSLSTM QVQGAAGGGV TAGGTQGGF ITSATVGEVS VAKLAPPAKN GWQWWLSGTP YGQELWALLS VKAVGGFYIG GLPERRGFRK VGGTFW UniProtKB: Phage protein |
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
---|---|
Grid | Model: Quantifoil R2/2 / Material: COPPER / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | TFS KRIOS |
---|---|
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number real images: 12520 / Average electron dose: 34.4 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | C2 aperture diameter: 100.0 µm / Calibrated defocus max: 1.75 µm / Calibrated defocus min: 0.75 µm / Calibrated magnification: 64000 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.75 µm / Nominal defocus min: 0.75 µm / Nominal magnification: 64000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |