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Cryo-EM structure of the bacteriophage T4 portal protein assembly at near-atomic resolution.

Sun L, Zhang X, Gao S, Rao PA, Padilla-Sanchez V, Chen Z, Sun S, Xiang Y, Subramaniam S, Rao VB, Rossmann MG - Nat Commun (2015)

Bottom Line: However, the detailed structure of the portal protein remained unknown.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.

View Article: PubMed Central - PubMed

Affiliation: Department of Biological Sciences, Purdue University, 240S. Martin Jischke Drive, West Lafayette, Indiana 47907-2032, USA.

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 3.6 Å 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.

No MeSH data available.


Related in: MedlinePlus

Interactions between the T4 gp20 portal and the gp17 ATPase.(a) Fitting of the T4 portal protein (purple) and gp17 (tan) into the 35 Å cryo-EM reconstruction of the procapsid+gp17 (EMD-1572 accession number). (b) Residues involved in the interaction between gp20 (purple) and gp17 (tan) are shown as sticks. (c) The surface charge of gp20 and gp17 around the interface area showing electrostatic interactions. The view orientation is the same as in panel (b).
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f5: Interactions between the T4 gp20 portal and the gp17 ATPase.(a) Fitting of the T4 portal protein (purple) and gp17 (tan) into the 35 Å cryo-EM reconstruction of the procapsid+gp17 (EMD-1572 accession number). (b) Residues involved in the interaction between gp20 (purple) and gp17 (tan) are shown as sticks. (c) The surface charge of gp20 and gp17 around the interface area showing electrostatic interactions. The view orientation is the same as in panel (b).

Mentions: The structures of the T4 gp20 portal protein assembly and of the T4 large terminase gp17 ATPase were docked into the previously determined 35 Å resolution cryo-EM structure of the prolate prohead complexed with gp17 (ref. 6). The docked structure shows that the five gp17 ATPases bind to the portal protein assembly with no apparent contact between the gp17 molecules and the capsid protein (Fig. 5a). The area of contact between the ring of twelve gp20 molecules and the five gp17 molecules involves primarily electrostatic interactions.


Cryo-EM structure of the bacteriophage T4 portal protein assembly at near-atomic resolution.

Sun L, Zhang X, Gao S, Rao PA, Padilla-Sanchez V, Chen Z, Sun S, Xiang Y, Subramaniam S, Rao VB, Rossmann MG - Nat Commun (2015)

Interactions between the T4 gp20 portal and the gp17 ATPase.(a) Fitting of the T4 portal protein (purple) and gp17 (tan) into the 35 Å cryo-EM reconstruction of the procapsid+gp17 (EMD-1572 accession number). (b) Residues involved in the interaction between gp20 (purple) and gp17 (tan) are shown as sticks. (c) The surface charge of gp20 and gp17 around the interface area showing electrostatic interactions. The view orientation is the same as in panel (b).
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4493910&req=5

f5: Interactions between the T4 gp20 portal and the gp17 ATPase.(a) Fitting of the T4 portal protein (purple) and gp17 (tan) into the 35 Å cryo-EM reconstruction of the procapsid+gp17 (EMD-1572 accession number). (b) Residues involved in the interaction between gp20 (purple) and gp17 (tan) are shown as sticks. (c) The surface charge of gp20 and gp17 around the interface area showing electrostatic interactions. The view orientation is the same as in panel (b).
Mentions: The structures of the T4 gp20 portal protein assembly and of the T4 large terminase gp17 ATPase were docked into the previously determined 35 Å resolution cryo-EM structure of the prolate prohead complexed with gp17 (ref. 6). The docked structure shows that the five gp17 ATPases bind to the portal protein assembly with no apparent contact between the gp17 molecules and the capsid protein (Fig. 5a). The area of contact between the ring of twelve gp20 molecules and the five gp17 molecules involves primarily electrostatic interactions.

Bottom Line: However, the detailed structure of the portal protein remained unknown.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.

View Article: PubMed Central - PubMed

Affiliation: Department of Biological Sciences, Purdue University, 240S. Martin Jischke Drive, West Lafayette, Indiana 47907-2032, USA.

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 3.6 Å 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.

No MeSH data available.


Related in: MedlinePlus