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Open data
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Basic information
Entry | Database: PDB / ID: 8k35 | |||||||||||||||
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Title | Structure of the bacteriophage lambda tail tip complex | |||||||||||||||
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![]() | VIRAL PROTEIN / Complex | |||||||||||||||
Function / homology | ![]() virus tail, tube / symbiont genome ejection through host cell envelope, long flexible tail mechanism / viral tail assembly / virus tail / 4 iron, 4 sulfur cluster binding / host cell cytoplasm / entry receptor-mediated virion attachment to host cell / receptor-mediated virion attachment to host cell / virion attachment to host cell / metal ion binding Similarity search - Function | |||||||||||||||
Biological species | ![]() | |||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.44 Å | |||||||||||||||
![]() | Xiao, H. / Tan, L. / Cheng, L.P. / Liu, H.R. | |||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of the siphophage neck-Tail complex suggests that conserved tail tip proteins facilitate receptor binding and tail assembly. Authors: Hao Xiao / Le Tan / Zhixue Tan / Yewei Zhang / Wenyuan Chen / Xiaowu Li / Jingdong Song / Lingpeng Cheng / Hongrong Liu / ![]() Abstract: Siphophages have a long, flexible, and noncontractile tail that connects to the capsid through a neck. The phage tail is essential for host cell recognition and virus-host cell interactions; ...Siphophages have a long, flexible, and noncontractile tail that connects to the capsid through a neck. The phage tail is essential for host cell recognition and virus-host cell interactions; moreover, it serves as a channel for genome delivery during infection. However, the in situ high-resolution structure of the neck-tail complex of siphophages remains unknown. Here, we present the structure of the siphophage lambda "wild type," the most widely used, laboratory-adapted fiberless mutant. The neck-tail complex comprises a channel formed by stacked 12-fold and hexameric rings and a 3-fold symmetrical tip. The interactions among DNA and a total of 246 tail protein molecules forming the tail and neck have been characterized. Structural comparisons of the tail tips, the most diversified region across the lambda and other long-tailed phages or tail-like machines, suggest that their tail tip contains conserved domains, which facilitate tail assembly, receptor binding, cell adsorption, and DNA retaining/releasing. These domains are distributed in different tail tip proteins in different phages or tail-like machines. The side tail fibers are not required for the phage particle to orient itself vertically to the surface of the host cell during attachment. | |||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 938.5 KB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.3 MB | Display | ![]() |
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Full document | ![]() | 1.3 MB | Display | |
Data in XML | ![]() | 124 KB | Display | |
Data in CIF | ![]() | 190 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 36844MC ![]() 8k36C ![]() 8k37C ![]() 8k38C ![]() 8k39C M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Components
-Protein , 4 types, 15 molecules IABxKQLRTUVWPMS
#1: Protein | Mass: 124550.625 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | Mass: 23146.590 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | Mass: 25831.779 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein | Mass: 92393.430 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Tail tip protein ... , 2 types, 9 molecules JGNHOCEDF
#2: Protein | Mass: 25730.578 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Protein | Mass: 12547.373 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 1 types, 3 molecules ![](data/chem/img/SF4.gif)
#7: Chemical |
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-Details
Has ligand of interest | N |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: Escherichia phage Lambda / Type: VIRUS / Entity ID: #1-#6 / Source: NATURAL |
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Source (natural) | Organism: ![]() |
Details of virus | Empty: NO / Enveloped: NO / Isolate: SPECIES / Type: VIRION |
Buffer solution | pH: 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2200 nm / Nominal defocus min: 1600 nm |
Image recording | Electron dose: 32 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
CTF correction | Type: PHASE FLIPPING ONLY | ||||||||||||||||||||||||
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3D reconstruction | Resolution: 3.44 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 54385 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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