+
Open data
-
Basic information
Entry | ![]() | |||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Title | Mycobacteriophage Bxb1 Capsid - Composite map and model | |||||||||||||||||||||||||||
![]() | Mycobacteriophage Bxb1 Capsid - Composite map and model | |||||||||||||||||||||||||||
![]() |
| |||||||||||||||||||||||||||
![]() | Bacteriophage / capsid / VIRUS / VIRAL PROTEIN | |||||||||||||||||||||||||||
Function / homology | : / Phage capsid / Phage capsid family / virion component / Major capsid 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 | ![]() | 1.2 GB | ![]() | |
---|---|---|---|---|
Header (meta data) | ![]() ![]() | 16.3 KB 16.3 KB | Display Display | ![]() |
Images | ![]() | 175.4 KB | ||
Filedesc metadata | ![]() | 6.1 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 489.7 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 489.2 KB | Display | |
Data in XML | ![]() | 10.1 KB | Display | |
Data in CIF | ![]() | 11.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9d9xMC ![]() 9d93C ![]() 9d94C ![]() 9d9lC ![]() 9d9wC C: citing same article ( M: atomic model generated by this map |
---|---|
Similar structure data | Similarity search - Function & homology ![]() |
-
Links
EMDB pages | ![]() ![]() |
---|---|
Related items in Molecule of the Month |
-
Map
File | ![]() | ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Mycobacteriophage Bxb1 Capsid - Composite map and model | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.32 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: Major capsid protein
Macromolecule | Name: Major capsid protein / type: protein_or_peptide / ID: 1 / Number of copies: 11 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 41.875461 KDa |
Sequence | String: MGFSADHSQI AQTKDTMFTG YLDPVQAKDY FAEAEKTSIV QRVAQKIPMG ATGIVIPHWT GDVSAQWIGE GDMKPITKGN MTKRDVHPA KIATIFVASA ETVRANPANY LGTMRTKVAT AIAMAFDNAA LHGTNAPSAF QGYLDQSNKT QSISPNAYQG L GVSGLTKL ...String: MGFSADHSQI AQTKDTMFTG YLDPVQAKDY FAEAEKTSIV QRVAQKIPMG ATGIVIPHWT GDVSAQWIGE GDMKPITKGN MTKRDVHPA KIATIFVASA ETVRANPANY LGTMRTKVAT AIAMAFDNAA LHGTNAPSAF QGYLDQSNKT QSISPNAYQG L GVSGLTKL VTDGKKWTHT LLDDTVEPVL NGSVDANGRP LFVESTYESL TTPFREGRIL GRPTILSDHV AEGDVVGYAG DF SQIIWGQ VGGLSFDVTD QATLNLGSQE SPNFVSLWQH NLVAVRVEAE YGLLINDVNA FVKLTFDPVL TTYALDLDGA SAG NFTLSL DGKTSANIAY NASTATVKSA IVAIDDGVSA DDVTVTGSAG DYTITVPGTL TADFSGLTDG EGASISVVSV G UniProtKB: Major capsid 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-PROPANE / Chamber humidity: 100 % / Chamber temperature: 283 K / Instrument: FEI VITROBOT MARK IV |
-
Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / 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: 2.5 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
-
Image processing
Startup model | Type of model: INSILICO MODEL |
---|---|
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.0 Å / Resolution method: OTHER / Number images used: 23927 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |