Abstract
The structure and assembly of bacteriophage T4 has been extensively studied. However, the detailed structure of the portal protein remained unknown. Here we report the structure of the bacteriophage T4 portal assembly, gene product 20 (gp20), determined by cryo-electron microscopy (cryo-EM) to 3.6Å resolution. In addition, analysis of a 10 Å resolution cryo-EM map of an empty prolate T4 head shows how the dodecameric portal assembly interacts with the capsid protein gp23 at the special pentameric vertex. The gp20 structure also verifies that the portal assembly is required for initiating head assembly, for attachment of the packaging motor, and for participation in DNA packaging. Comparison of the Myoviridae T4 portal structure with the known portal structures of φ29, SPP1 and P22, representing Podo-and Siphoviridae, shows that the portal structure probably dates back to a time when self-replicating microorganisms were being established on Earth.
| Original language | English (US) |
|---|---|
| Article number | 7548 |
| Journal | Nature Communications |
| Volume | 6 |
| DOIs | |
| State | Published - Jul 6 2015 |
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ASJC Scopus subject areas
- Chemistry(all)
- Biochemistry, Genetics and Molecular Biology(all)
- Physics and Astronomy(all)
Cite this
Cryo-EM structure of the bacteriophage T4 portal protein assembly at near-atomic resolution. / Sun, Lei; Zhang, Xinzheng; Gao, Song; Rao, Prashant A.; Padilla-Sanchez, Victor; Chen, Zhenguo; Sun, Siyang; Xiang, Ye; Subramaniam, Sriram; Rao, Venigalla B.; Rossmann, Michael G.
In: Nature Communications, Vol. 6, 7548, 06.07.2015.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Cryo-EM structure of the bacteriophage T4 portal protein assembly at near-atomic resolution
AU - Sun, Lei
AU - Zhang, Xinzheng
AU - Gao, Song
AU - Rao, Prashant A.
AU - Padilla-Sanchez, Victor
AU - Chen, Zhenguo
AU - Sun, Siyang
AU - Xiang, Ye
AU - Subramaniam, Sriram
AU - Rao, Venigalla B.
AU - Rossmann, Michael G.
PY - 2015/7/6
Y1 - 2015/7/6
N2 - The structure and assembly of bacteriophage T4 has been extensively studied. However, the detailed structure of the portal protein remained unknown. Here we report the structure of the bacteriophage T4 portal assembly, gene product 20 (gp20), determined by cryo-electron microscopy (cryo-EM) to 3.6Å resolution. In addition, analysis of a 10 Å resolution cryo-EM map of an empty prolate T4 head shows how the dodecameric portal assembly interacts with the capsid protein gp23 at the special pentameric vertex. The gp20 structure also verifies that the portal assembly is required for initiating head assembly, for attachment of the packaging motor, and for participation in DNA packaging. Comparison of the Myoviridae T4 portal structure with the known portal structures of φ29, SPP1 and P22, representing Podo-and Siphoviridae, shows that the portal structure probably dates back to a time when self-replicating microorganisms were being established on Earth.
AB - The structure and assembly of bacteriophage T4 has been extensively studied. However, the detailed structure of the portal protein remained unknown. Here we report the structure of the bacteriophage T4 portal assembly, gene product 20 (gp20), determined by cryo-electron microscopy (cryo-EM) to 3.6Å resolution. In addition, analysis of a 10 Å resolution cryo-EM map of an empty prolate T4 head shows how the dodecameric portal assembly interacts with the capsid protein gp23 at the special pentameric vertex. The gp20 structure also verifies that the portal assembly is required for initiating head assembly, for attachment of the packaging motor, and for participation in DNA packaging. Comparison of the Myoviridae T4 portal structure with the known portal structures of φ29, SPP1 and P22, representing Podo-and Siphoviridae, shows that the portal structure probably dates back to a time when self-replicating microorganisms were being established on Earth.
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UR - http://www.scopus.com/inward/citedby.url?scp=84936116751&partnerID=8YFLogxK
U2 - 10.1038/ncomms8548
DO - 10.1038/ncomms8548
M3 - Article
C2 - 26144253
AN - SCOPUS:84936116751
VL - 6
JO - Nature Communications
JF - Nature Communications
SN - 2041-1723
M1 - 7548
ER -