1N7V

THE RECEPTOR-BINDING PROTEIN P2 OF BACTERIOPHAGE PRD1: CRYSTAL FORM III

Summary for 1N7V

• Entry DOI: 10.2210/pdb1n7v/pdb
• Related: 1N7U
• Descriptor: Adsorption protein P2, ACETATE ION, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: bacteriophage prd1, viral receptor-binding, beta-propeller, proline-rich, antibiotic-resistance, viral protein
• Biological source: Enterobacteria phage PRD1
• Cellular location: Virion: P27378
• Total number of polymer chains: 1
• Total formula weight: 60083.58

Authors

Xu, L.,Benson, S.D.,Butcher, S.J.,Bamford, D.H.,Burnett, R.M. (deposition date: 2002-11-18, release date: 2003-04-08, Last modification date: 2024-02-14)

Primary citation

Xu, L.,Benson, S.D.,Butcher, S.J.,Bamford, D.H.,Burnett, R.M.
The Receptor Binding Protein P2 of PRD1, a Virus Targeting Antibiotic-Resistant Bacteria, Has a Novel Fold Suggesting Multiple Functions.
Structure, 11:309-322, 2003

PubMed Abstract: 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 A 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.

PubMed: 12623018
DOI: 10.1016/S0969-2126(03)00023-6

Experimental method

X-RAY DIFFRACTION (2.2 Å)