[English] 日本語

- EMDB-46669: Mycobacteriophage Bxb1 portal and connector assembly - Composite ... -
+
Open data
-
Basic information
Entry | ![]() | |||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Title | Mycobacteriophage Bxb1 portal and connector assembly - Composite map and model | |||||||||||||||||||||||||||
![]() | Mycobacteriophage Bxb1 portal and connector assembly - Composite map and model | |||||||||||||||||||||||||||
![]() |
| |||||||||||||||||||||||||||
![]() | Bacteriophage / portal / VIRAL PROTEIN | |||||||||||||||||||||||||||
Function / homology | Mycobacteriophage D29, Gp19 / Phage protein Gp19/Gp15/Gp42 / Portal protein / Phage portal protein, SPP1 Gp6-like / Tail terminator / Major tail protein / Head-to-tail stopper / Head-to-tail adaptor / Portal protein![]() | |||||||||||||||||||||||||||
Biological species | ![]() | |||||||||||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.0 Å | |||||||||||||||||||||||||||
![]() | Freeman KG / White SJ / Huet A / Conway JF | |||||||||||||||||||||||||||
Funding support | ![]() ![]()
| |||||||||||||||||||||||||||
![]() | ![]() Title: Structure and infection dynamics of mycobacteriophage Bxb1. Authors: Krista G Freeman / Sudipta Mondal / Lourriel S Macale / Jennifer Podgorski / Simon J White / Benjamin H Silva / Valery Ortiz / Alexis Huet / Ronelito J Perez / Joemark T Narsico / Meng-Chiao ...Authors: Krista G Freeman / Sudipta Mondal / Lourriel S Macale / Jennifer Podgorski / Simon J White / Benjamin H Silva / Valery Ortiz / Alexis Huet / Ronelito J Perez / Joemark T Narsico / Meng-Chiao Ho / Deborah Jacobs-Sera / Todd L Lowary / James F Conway / Donghyun Park / Graham F Hatfull / ![]() ![]() Abstract: Mycobacteriophage Bxb1 is a well-characterized virus of Mycobacterium smegmatis with double-stranded DNA and a long, flexible tail. Mycobacteriophages show considerable potential as therapies for ...Mycobacteriophage Bxb1 is a well-characterized virus of Mycobacterium smegmatis with double-stranded DNA and a long, flexible tail. Mycobacteriophages show considerable potential as therapies for Mycobacterium infections, but little is known about the structural details of these phages or how they bind to and traverse the complex Mycobacterium cell wall. Here, we report the complete structure and atomic model of phage Bxb1, including the arrangement of immunodominant domains of both the capsid and tail tube subunits, as well as the assembly of the protein subunits in the tail-tip complex. The structure contains protein assemblies with 3-, 5-, 6-, and 12-fold symmetries, which interact to satisfy several symmetry mismatches. Cryoelectron tomography of phage particles bound to M. smegmatis reveals the structural transitions that occur for free phage particles to bind to the cell surface and navigate through the cell wall to enable DNA transfer into the cytoplasm. | |||||||||||||||||||||||||||
History |
|
-
Structure visualization
Supplemental images |
---|
-
Downloads & links
-EMDB archive
Map data | ![]() | 354.6 MB | ![]() | |
---|---|---|---|---|
Header (meta data) | ![]() ![]() | 22.1 KB 22.1 KB | Display Display | ![]() |
Images | ![]() | 120.2 KB | ||
Filedesc metadata | ![]() | 6.9 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9d94MC ![]() 9d93C ![]() 9d9lC ![]() 9d9wC ![]() 9d9xC C: citing same article ( M: atomic model generated by this map |
---|---|
Similar structure data | Similarity search - Function & homology ![]() |
-
Links
EMDB pages | ![]() ![]() |
---|
-
Map
File | ![]() | ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Mycobacteriophage Bxb1 portal and connector assembly - Composite map and model | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.12 Å | ||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-
Sample components
-Entire : Mycobacterium phage Bxb1
Entire | Name: ![]() |
---|---|
Components |
|
-Supramolecule #1: Mycobacterium phage Bxb1
Supramolecule | Name: Mycobacterium phage Bxb1 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all Details: Portal and connector complex of Bxb1, containing five protein subunit types. This is a composite map, and related entries for consensus and locally refined maps are noted. NCBI-ID: 2902907 / Sci species name: Mycobacterium phage Bxb1 / Sci species strain: Mycobacterium phage Bxb1 / Virus type: VIRION / Virus isolate: SPECIES / Virus enveloped: No / Virus empty: No |
---|---|
Host (natural) | Organism: ![]() |
-Macromolecule #1: Portal protein
Macromolecule | Name: Portal protein / type: protein_or_peptide / ID: 1 / Number of copies: 12 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 53.822113 KDa |
Sequence | String: MAETESIDPE KLRDQLLDAF ENKQNELKSS KAYYDAERRP DAIGLAVPLD MRKYLAHVGY PRTYVDAIAE RQELEGFRIP SANGEEPES GGENDPASEL WDWWQANNLD IEATLGHTDA LIYGTAYITI SMPDPEVDFD VDPEVPLIRV EPPTALYAEV D PRTRKVLY ...String: MAETESIDPE KLRDQLLDAF ENKQNELKSS KAYYDAERRP DAIGLAVPLD MRKYLAHVGY PRTYVDAIAE RQELEGFRIP SANGEEPES GGENDPASEL WDWWQANNLD IEATLGHTDA LIYGTAYITI SMPDPEVDFD VDPEVPLIRV EPPTALYAEV D PRTRKVLY AIRAIYGADG NEIVSATLYL PDTTMTWLRA EGEWEAPTST PHGLEMVPVI PISNRTRLSD LYGTSEISPE LR SVTDAAA QILMNMQGTA NLMAIPQRLI FGAKPEELGI NAETGQRMFD AYMARILAFE GGEGAHAEQF SAAELRNFVD ALD ALDRKA ASYSGLPPQY LSSSSDNPAS AEAIKAAESR LVKKVERKNK IFGGAWEQAM RLAYKMVKGG DIPTEYYRME TVWR DPSTP TYAAKADAAA KLFANGAGLI PRERGWVDMG YTIVEREQMR QWLEQDQKQG LGLIGSLYGA STPEGKPGEA PVGEP PAPE PDAA UniProtKB: Portal protein |
-Macromolecule #2: Head-to-tail adaptor
Macromolecule | Name: Head-to-tail adaptor / type: protein_or_peptide / ID: 2 / Number of copies: 12 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 14.064146 KDa |
Sequence | String: MATLATHEDV TAFWARTPTA EEIVLINRRL AQAERMLLRA IPELLIKASS DPVFRAEVID IEAEAVLRLV RNHEGYLSET DGNYTYMLQ AQDPNRKLEI LPEEWEVLGI VRSGLGILVP TVVLPS UniProtKB: Head-to-tail adaptor |
-Macromolecule #3: Head-to-tail stopper
Macromolecule | Name: Head-to-tail stopper / type: protein_or_peptide / ID: 3 / Number of copies: 6 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 14.302012 KDa |
Sequence | String: MSLLDRGGTY GSPEDGFDPV TVYPEVTRKD RLGNTLVGPS LTGIETVARF QVQGQSGTSA RRAEMDDIGD MTEQVYTMRL PRSFTTELK SGSEVVWRGE RWGVYGEPRR YKGSRRIAHL EYTVRRF UniProtKB: Head-to-tail stopper |
-Macromolecule #4: Tail terminator
Macromolecule | Name: Tail terminator / type: protein_or_peptide / ID: 4 / Number of copies: 6 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 16.230531 KDa |
Sequence | String: MAGKLPIVGE VVLPILRGHE DLSNPISTVP SLAGVHVGTW VEDIDSRTFP LITVRRVGGT RSPEHPTLFT QPVVEMTAYS AADLPTTEQ MYEDALEVLY RAARLQTKTP AGYLHSVTET LGASHGPSPF DRTWRVFGLI RLGIRPPKN UniProtKB: Tail terminator |
-Macromolecule #5: Major tail protein
Macromolecule | Name: Major tail protein / type: protein_or_peptide / ID: 5 / Number of copies: 12 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 30.170271 KDa |
Sequence | String: MALKDDAVLI AARGYVYTAA VGTAAPTPSQ LKLIDLEHPE AWDRTGWDLV GHTSEDDLPE FGFDGGDSEV RGSWQKKKLR EVETEEIAD YVVINLTQFD ETALELYFGP NQSATPGIFG VKSGSVVNER ALLIVIVDND VRLGFHARKA SLKREDAISL A TDEFGALP ...String: MALKDDAVLI AARGYVYTAA VGTAAPTPSQ LKLIDLEHPE AWDRTGWDLV GHTSEDDLPE FGFDGGDSEV RGSWQKKKLR EVETEEIAD YVVINLTQFD ETALELYFGP NQSATPGIFG VKSGSVVNER ALLIVIVDND VRLGFHARKA SLKREDAISL A TDEFGALP VRATFLDYQS YNLYEWIEED WFNAVDAPVV YLLDLGGATG GDYTLLVGGK STGDIAYNAN ASAIKTAIGA VD DGVAESA WTVTADGSDF EISGPLAVAL GVDSTTGGSG VTVDVV UniProtKB: Major tail protein |
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
![]() | single particle reconstruction |
Aggregation state | particle |
-
Sample preparation
Concentration | 10 mg/mL | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Buffer | pH: 7.5 Component:
| |||||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 283.15 K / Instrument: FEI VITROBOT MARK IV |
-
Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 30.0 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: 0.8 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |