1n7u
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(New page: 200px<br /><applet load="1n7u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n7u, resolution 2.40Å" /> '''THE RECEPTOR-BINDING...)
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Revision as of 19:54, 20 November 2007
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THE RECEPTOR-BINDING PROTEIN P2 OF BACTERIOPHAGE PRD1: CRYSTAL FORM I
Overview
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.
About this Structure
1N7U is a Single protein structure of sequence from Enterobacteria phage prd1 with ACT and CA as ligands. Full crystallographic information is available from OCA.
Reference
The receptor binding protein P2 of PRD1, a virus targeting antibiotic-resistant bacteria, has a novel fold suggesting multiple functions., Xu L, Benson SD, Butcher SJ, Bamford DH, Burnett RM, Structure. 2003 Mar;11(3):309-22. PMID:12623018
Page seeded by OCA on Tue Nov 20 22:01:57 2007
