Regensburg 2010 – scientific programme
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CPP: Fachverband Chemische Physik und Polymerphysik
CPP 16: Nuclear Magnetic Resonance: Frontiers and Applications
CPP 16.10: Talk
Tuesday, March 23, 2010, 16:00–16:15, H48
Structure of Phage SPP1 Head-to-Tail Connector Reveals Gating Mechanism for DNA Ejection: an EM and NMR study — Matthieu Gallopin1, Sophie Lhuillier2, Bernard Gilquin1, Sandrine Brasilès2, Elena Orlova3, Joël Couprie1, Paulo Tavares2, and •Sophie Zinn-Justin1 — 1Laboratoire de Biologie Structurale et Radiobiologie, iBiTec-S, CEA Saclay, Gif-sur-Yvette, France — 2Unité de Virologie Moléculaire et Structurale, UMR CNRS 2472, UMR INRA 1157 and IFR 115, Gif-sur-Yvette, France — 3Department of Crystallography, Birkbeck College, University of London, London, UK
Understanding the principles that govern macromolecular assembly is a current challenge for biochemists, molecular biologists, and structural biologists. Assembly of bacterial virus (bacteriophages) particles is a highly suitable system to investigate the molecular mechanisms that support efficient formation of a complex macromolecular machine and its function. A large number of phages and eukaryotic viruses use a portal system to control genome entry and exit from their capsids. The portal and head completion proteins form the viral head-to-tail connector. The pseudo-atomic structure of the complete closed connector of tailed bacteriophage SPP1 was determined (Lhuillier et al., PNAS 2009). Opening of the connector and DNA ejection from virions was reproduced in vitro by adding the host purified receptor YueB. These achievements recommend SPP1 as an excellent system to investigate the structural organization and dynamics of the viral DNA gatekeeper.