Journal
STRUCTURE
Volume 11, Issue 3, Pages 309-322Publisher
CELL PRESS
DOI: 10.1016/S0969-2126(03)00023-6
Keywords
antibiotic resistance; bacteriophage PRD1; receptor binding protein; Tectiviridae; X-ray crystallography
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Bacteriophage PRD1 is unusual, with an internal lipid membrane, but has striking resemblances to adenovirus that include receptor binding spikes. The PRD1 vertex complex contains P2, a 590 residue monomer that binds to receptors on antibiotic-resistant strains of E coli and so is the functional counterpart to adenovirus fiber. P2 structures from two crystal forms, at 2.2 and 2.4 Angstrom resolution, reveal an elongated club-shaped molecule with a novel beta propeller head showing pseudo-6-fold symmetry. An extended loop with another novel fold forms a long tail containing a protruding proline-rich fin. The head and fin structures are well suited to recognition and attachment, and the tail is likely to trigger the processes of vertex disassembly, membrane tube formation, and subsequent DNA injection.
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