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Open data
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Basic information
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Title | Baseplate structure of Escherichia phage Mu | ||||||||||||
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![]() | phage / sheath / tube / VIRAL PROTEIN | ||||||||||||
Function / homology | ![]() viral genome circularization / symbiont-mediated evasion of DNA end degradation by host / viral tropism switching / virus tail, sheath / symbiont genome ejection through host cell envelope, contractile tail mechanism / virus tail, tube / virus tail, baseplate / virus tail, fiber / viral tail assembly / adhesion receptor-mediated virion attachment to host cell ...viral genome circularization / symbiont-mediated evasion of DNA end degradation by host / viral tropism switching / virus tail, sheath / symbiont genome ejection through host cell envelope, contractile tail mechanism / virus tail, tube / virus tail, baseplate / virus tail, fiber / viral tail assembly / adhesion receptor-mediated virion attachment to host cell / : / virion component / host cell cytoplasm / symbiont-mediated suppression of host innate immune response / symbiont entry into host cell / DNA binding / metal ion binding Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.3 Å | ||||||||||||
![]() | Zhou JQ / Liu HR | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: structures of the contractile nanomachine myophage Mu in both its extended and contracted states. Authors: Junquan Zhou / Liwen Wang / Hao Xiao / Wenyuan Chen / Zhonghua Liu / Jingdong Song / Jing Zheng / Hongrong Liu / ![]() Abstract: Myophage Mu is a representative of contractile nanomachines with a simple tail baseplate. It has the capacity to infect a range of intestinal bacteria and has extensive applications in genetic ...Myophage Mu is a representative of contractile nanomachines with a simple tail baseplate. It has the capacity to infect a range of intestinal bacteria and has extensive applications in genetic engineering research. Nevertheless, a comprehensive understanding of the entire structure and contractile mechanisms of Mu remains elusive. Using cryo-electron microscopy (cryo-EM), we resolved the asymmetric structures of Mu in both its extended and contracted states, the latter of which lacked the tail baseplate, at near-atomic resolutions. We built the atomic models for the extended Mu, encompassing the head, the connector complex, the tail, and the simple baseplate. It is noteworthy that we identified the position and structure of the tail tube initiator protein gp43 (referred to as the DNA circularization protein). The protein gp43 plays a crucial role not only in the baseplate assembly and DNA circularization but also in stabilizing the wedge-hub connection and mediating tail contraction. Except for the baseplate structure, the structural comparison of Mu in its extended and contracted states revealed that only the tail sheath protein gp39 and the C-terminus of the tail terminator protein gp37 undergo notable conformational changes to accommodate the tail contraction, whereas the remaining protein components remained unchanged. Our structures exhibited conserved properties among the majority of myophages, thereby providing valuable insights into the contraction mechanisms across myophages and contractile injection systems (CISs). IMPORTANCE: Despite extensive study, the asymmetric structures of phage Mu, a highly effective transposable myophage, remain unknown. In this study, we present the high-resolution structures of Mu in ...IMPORTANCE: Despite extensive study, the asymmetric structures of phage Mu, a highly effective transposable myophage, remain unknown. In this study, we present the high-resolution structures of Mu in both its extended and contracted states. The comparison of the two structures allows for the illustration of detailed conformational changes of the head-to-tail complex during the process of tail contraction. The contraction mechanism of Mu is highly conserved and widely adapted to all contractile nanomachines that share common structural features with Mu. | ||||||||||||
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Structure visualization
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Downloads & links
-EMDB archive
Map data | ![]() | 95.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 27.1 KB 27.1 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 10.6 KB | Display | ![]() |
Images | ![]() | 105.9 KB | ||
Masks | ![]() | 103 MB | ![]() | |
Filedesc metadata | ![]() | 8.2 KB | ||
Others | ![]() ![]() | 80.4 MB 80.4 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9ki1MC ![]() 9jodC ![]() 9khxC ![]() 9khyC ![]() 9knuC ![]() 9lj8C M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.36 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Density Histograms |
-Half map: #2
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Density Histograms |
-Half map: #1
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Density Histograms |
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Sample components
+Entire : Escherichia phage Mu
+Supramolecule #1: Escherichia phage Mu
+Macromolecule #1: DNA circularization protein N
+Macromolecule #2: Tail sheath protein
+Macromolecule #3: Tail tube protein
+Macromolecule #4: Baseplate protein gp46
+Macromolecule #5: Baseplate hub protein gp44
+Macromolecule #6: Baseplate protein gp47
+Macromolecule #7: Baseplate puncturing device gp45
+Macromolecule #8: Baseplate protein gp48
+Macromolecule #9: Probable tape measure protein
+Macromolecule #10: Tail fiber protein S
+Macromolecule #11: CALCIUM ION
+Macromolecule #12: FE (III) ION
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 35.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 4.0 µm / Nominal defocus min: 2.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |