Structural framework for DNA translocation via the viral portal protein
Identifieur interne : 001C49 ( Istex/Curation ); précédent : 001C48; suivant : 001C50Structural framework for DNA translocation via the viral portal protein
Auteurs : Andrey A. Lebedev [Royaume-Uni] ; Margret H. Krause [Allemagne] ; Anabela L. Isidro [France, Portugal] ; Alexei A. Vagin [Royaume-Uni] ; Elena V. Orlova [Royaume-Uni] ; Joanne Turner [Royaume-Uni] ; Eleanor J. Dodson [Royaume-Uni] ; Paulo Tavares [France] ; Alfred A. Antson [Royaume-Uni]Source :
- The EMBO Journal [ 0261-4189 ] ; 2007-04-04.
English descriptors
- Teeft :
- Acta crystallogr, Adjacent subunits, Atpase, Bacillus subtilis bacteriophage spp1, Bacteriophage, Bacteriophage spp1, Base pairs, Biol, Biology organization spp1 portal protein structure, Capsid, Central tunnel, Conformation, Conformational changes, Connector, Constricted part, Contact area, Crystallogr, Cyan, Direct hydrogen bonds, Dube, Embo, Embo journal, Energy minima, Groove, Helix, Isidro, Lebedev, Long helix, Loop, Loop positions, Lurz, Major groove, Mechanistic model, Molecular lever, Molecular motor, Molecular replacement, Morais, Mutation, Oliveira, Orlova, Packaging motor, Pathway, Phage, Portal, Portal protein, Portal proteins, Procapsid, Protein, Pseudoatomic, Pseudoatomic structure, Relative rotation, Rigid bodies, Scaffolding protein, Search model, Single subunit, Spp1, Spp1 portal protein, Spp1 portal protein structure, Structural data, Structural observations, Subunit, Supplementary movie, Symmetry constraints, Tavares, Translation function, Translocation, Tting, Tunnel, Tunnel axis, Tunnel loop, Tunnel loops, Viral, Viral atpase, Viral particle assembly.
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.
Url:
DOI: 10.1038/sj.emboj.7601643
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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.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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