3j4b

Structure of T7 gatekeeper protein (gp11)Structure of T7 gatekeeper protein (gp11)

3j4b, resolution 12.00Å Show:Asymmetric Unit Biological Assembly Structural highlights 3j4b is a 12 chain structure with sequence from Escherichia phage T7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 12Å Experimental data: Check Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TUBE1_BPT7 Structural component of the short non-contractile tail. The tail complex is involved in viral genome delivery. Forms the 12-fold symmetric toroidal domain immediately below the connector protein gp8. Once the tail tubular structure is formed, the interface between gp11 and gp12 generates the proper environment to interact with the six fibers, each made of gp17 trimers. Publication Abstract from PubMed Most bacterial viruses need aspecialized machinery, called "tail", to inject their genomes inside the bacterial cytoplasm without disrupting the cellular integrity. Bacteriophage T7 is a well-characterized member of the Podoviridae family infecting Escherichia coli (E. coli), and it has a short non-contractile tail that assembles sequentially on the viral head after DNA packaging. The T7 tail is a complex of around 2.7 MDa composed of at least four proteins: the connector (gene product 8, gp8), the tail tubular proteins gp11 and gp12 and the fibres (gp17). Using cryo-electron microscopy (cryo-EM) and single particle image reconstruction techniques, we have determined the precise topology of the tail proteins by comparing the structure of the T7 tail extracted from viruses and a complex formed by recombinant gp8, gp11 and gp12 proteins. Furthermore, the order of assembly of the structural components within the complex was deduced from interaction assays with cloned and purified tail proteins. The existence of common folds among similar tail proteins allowed us to obtain pseudo-atomic threaded models of gp8 (connector) and gp11 (gatekeeper) proteins, which were docked into the corresponding cryo-EM volumes of the tail complex. This pseudo-atomic model of the connector-gatekeeper interaction revealed the existence of a common molecular architecture among viruses belonging to the three tailed bacteriophage families, strongly suggesting that a common molecular mechanism has been favoured during evolution to coordinate the transition between DNA packaging and tail assembly. Structural Characterization Of The Bacteriophage T7 Tail Machinery.,Cuervo A, Pulido-Cid M, Chagoyen M, Arranz R, Gonzalez-Garcia VA, Garcia-Doval C, Caston JR, Valpuesta JM, van Raaij MJ, Martin-Benito J, Carrascosa JL J Biol Chem. 2013 Jul 24. PMID:23884409 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.