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TitleThe P22 tail machine at subnanometer resolution reveals the architecture of an infection conduit.
Journal, issue, pagesStructure, Vol. 17, Issue 6, Page 789-799, Year 2009
Publish dateJun 10, 2009
AuthorsGabriel C Lander / Reza Khayat / Rui Li / Peter E Prevelige / Clinton S Potter / Bridget Carragher / John E Johnson /
PubMed AbstractThe portal channel is a key component in the life cycle of bacteriophages and herpesviruses. The bacteriophage P22 portal is a 1 megadalton dodecameric oligomer of gp1 that plays key roles in capsid ...The portal channel is a key component in the life cycle of bacteriophages and herpesviruses. The bacteriophage P22 portal is a 1 megadalton dodecameric oligomer of gp1 that plays key roles in capsid assembly, DNA packaging, assembly of the infection machinery, and DNA ejection. The portal is the nucleation site for the assembly of 39 additional subunits generated from multiple copies of four gene products (gp4, gp10, gp9, and gp26), which together form the multifunctional tail machine. These components are organized with a combination of 12-fold (gp1, gp4), 6-fold (gp10, trimers of gp9), and 3-fold (gp26, gp9) symmetry. Here we present the 3-dimensional structures of the P22 assembly-naive portal formed from expressed subunits (gp1) and the intact tail machine purified from infectious virions. The assembly-naive portal structure exhibits a striking structural similarity to the structures of the portal proteins of SPP1 and phi29 derived from X-ray crystallography.
External linksStructure / PubMed:19523897 / PubMed Central
MethodsEM (single particle)
Resolution8.6 - 9.4 Å
Structure data

EMDB-5049:
12-fold assembly-naive P22 portal
Method: EM (single particle) / Resolution: 8.6 Å

EMDB-5050:
11-fold assembly-naive P22 portal
Method: EM (single particle) / Resolution: 8.6 Å

EMDB-5051:
P22 tail machine
Method: EM (single particle) / Resolution: 9.4 Å

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