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- PDB-8hqo: Neck of DT57C bacteriophage in the full state -

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Basic information

Entry
Database: PDB / ID: 8hqo
TitleNeck of DT57C bacteriophage in the full state
Components
  • Head completion protein
  • Portal protein
  • Tail terminator protein
  • Tape measure protein
KeywordsVIRAL PROTEIN / Neck / Portal / T5 / VIRUS
Function / homology
Function and homology information


: / Head completion protein / : / Bacteriophage Tail Tube Terminator Protein / : / : / Tape measure protein N-terminal / Tape measure protein C-terminal / Bacteriophage/Gene transfer agent portal protein / Phage portal protein
Similarity search - Domain/homology
Head completion protein / Portal protein / Tape measure protein / Tail terminator protein
Similarity search - Component
Biological speciesEscherichia phage DT57C (virus)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å
AuthorsAyala, R. / Moiseenko, A.V. / Chen, T.H. / Kulikov, E.E. / Golomidova, A.K. / Orekhov, P.S. / Street, M.A. / Sokolova, O.S. / Letarov, A.V. / Wolf, M.
Funding support Russian Federation, Japan, 4items
OrganizationGrant numberCountry
Russian Science Foundation21-44-07002 Russian Federation
Japan Society for the Promotion of Science (JSPS)21K20645 Japan
Japan Society for the Promotion of Science (JSPS)20K06581 Japan
Ministry of Agriculture, Forestry and Fisheries (MAFF)20320378 Japan
CitationJournal: Nat Commun / Year: 2023
Title: Nearly complete structure of bacteriophage DT57C reveals architecture of head-to-tail interface and lateral tail fibers.
Authors: Rafael Ayala / Andrey V Moiseenko / Ting-Hua Chen / Eugene E Kulikov / Alla K Golomidova / Philipp S Orekhov / Maya A Street / Olga S Sokolova / Andrey V Letarov / Matthias Wolf /
Abstract: The T5 family of viruses are tailed bacteriophages characterized by a long non-contractile tail. The bacteriophage DT57C is closely related to the paradigmal T5 phage, though it recognizes a ...The T5 family of viruses are tailed bacteriophages characterized by a long non-contractile tail. The bacteriophage DT57C is closely related to the paradigmal T5 phage, though it recognizes a different receptor (BtuB) and features highly divergent lateral tail fibers (LTF). Considerable portions of T5-like phages remain structurally uncharacterized. Here, we present the structure of DT57C determined by cryo-EM, and an atomic model of the virus, which was further explored using all-atom molecular dynamics simulations. The structure revealed a unique way of LTF attachment assisted by a dodecameric collar protein LtfC, and an unusual composition of the phage neck constructed of three protein rings. The tape measure protein (TMP) is organized within the tail tube in a three-stranded parallel α-helical coiled coil which makes direct contact with the genomic DNA. The presence of the C-terminal fragment of the TMP that remains within the tail tip suggests that the tail tip complex returns to its original state after DNA ejection. Our results provide a complete atomic structure of a T5-like phage, provide insights into the process of DNA ejection as well as a structural basis for the design of engineered phages and future mechanistic studies.
History
DepositionDec 13, 2022Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Dec 13, 2023Provider: repository / Type: Initial release
Revision 1.1Dec 27, 2023Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation_author.identifier_ORCID

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
D: Portal protein
E: Portal protein
R: Head completion protein
S: Head completion protein
a: Tail terminator protein
B: Portal protein
C: Portal protein
P: Head completion protein
Q: Head completion protein
b: Tail terminator protein
x: Tape measure protein


Theoretical massNumber of molelcules
Total (without water)427,71111
Polymers427,71111
Non-polymers00
Water00
1
D: Portal protein
E: Portal protein
R: Head completion protein
S: Head completion protein
a: Tail terminator protein
B: Portal protein
C: Portal protein
P: Head completion protein
Q: Head completion protein
b: Tail terminator protein
x: Tape measure protein

D: Portal protein
E: Portal protein
R: Head completion protein
S: Head completion protein
a: Tail terminator protein
B: Portal protein
C: Portal protein
P: Head completion protein
Q: Head completion protein
b: Tail terminator protein
x: Tape measure protein

D: Portal protein
E: Portal protein
R: Head completion protein
S: Head completion protein
a: Tail terminator protein
B: Portal protein
C: Portal protein
P: Head completion protein
Q: Head completion protein
b: Tail terminator protein
x: Tape measure protein


Theoretical massNumber of molelcules
Total (without water)1,283,13433
Polymers1,283,13433
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation2
MethodUCSF CHIMERA

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Components

#1: Protein
Portal protein


Mass: 45408.574 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Escherichia phage DT57C (virus) / References: UniProt: A0A0A7RUL5
#2: Protein
Head completion protein


Mass: 19203.900 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Escherichia phage DT57C (virus) / References: UniProt: A0A0A7RSP7
#3: Protein Tail terminator protein


Mass: 18317.475 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia phage DT57C (virus) / References: UniProt: A0A0A7RZ97
#4: Protein Tape measure protein


Mass: 132626.406 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia phage DT57C (virus) / References: UniProt: A0A0A7RZ92

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Tequintavirus DT57C / Type: VIRUS / Entity ID: all / Source: NATURAL
Source (natural)Organism: Tequintavirus DT57C
Details of virusEmpty: NO / Enveloped: NO / Isolate: SPECIES / Type: VIRION
Buffer solutionpH: 7
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE-PROPANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 4000 nm / Nominal defocus min: 1000 nm
Image recordingElectron dose: 67 e/Å2 / Film or detector model: FEI FALCON III (4k x 4k)

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Processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 34102 / Symmetry type: POINT

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