2JES

Portal protein (gp6) from bacteriophage SPP1

Summary for 2JES

• Entry DOI: 10.2210/pdb2jes/pdb
• Descriptor: PORTAL PROTEIN, UNIDENTIFIED FRAGMENT OF PORTAL PROTEIN, MERCURY (II) ION, ... (4 entities in total)
• Functional Keywords: bacteriophage spp1, dna translocation, molecular motor, viral portal protein, viral protein
• Biological source: BACTERIOPHAGE SPP1; More
• Cellular location: Virion : P54309
• Total number of polymer chains: 26
• Total formula weight: 782823.39

Authors

Lebedev, A.A.,Krause, M.H.,Isidro, A.L.,Vagin, A.A.,Orlova, E.V.,Turner, J.,Dodson, E.J.,Tavares, P.,Antson, A.A. (deposition date: 2007-01-21, release date: 2007-03-27, Last modification date: 2024-05-08)

Primary citation

Lebedev, A.A.,Krause, M.H.,Isidro, A.L.,Vagin, A.A.,Orlova, E.V.,Turner, J.,Dodson, E.J.,Tavares, P.,Antson, A.A.
Structural Framework for DNA Translocation Via the Viral Portal Protein
Embo J., 26:1984-, 2007

PubMed Abstract: Tailed bacteriophages and herpesviruses load their capsids with DNA through a tunnel formed by the portal protein assembly. Here we describe the X-ray structure of the bacteriophage SPP1 portal protein in its isolated 13-subunit form and the pseudoatomic structure of a 12-subunit assembly. The first defines the DNA-interacting segments (tunnel loops) that pack tightly against each other forming the most constricted part of the tunnel; the second shows that the functional dodecameric state must induce variability in the loop positions. Structural observations together with geometrical constraints dictate that in the portal-DNA complex, the loops form an undulating belt that fits and tightly embraces the helical DNA, suggesting that DNA translocation is accompanied by a 'mexican wave' of positional and conformational changes propagating sequentially along this belt.

PubMed: 17363899
DOI: 10.1038/SJ.EMBOJ.7601643

Experimental method

X-RAY DIFFRACTION (3.4 Å)