1n7u

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{{STRUCTURE_1n7u| PDB=1n7u | SCENE= }}
{{STRUCTURE_1n7u| PDB=1n7u | SCENE= }}
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'''THE RECEPTOR-BINDING PROTEIN P2 OF BACTERIOPHAGE PRD1: CRYSTAL FORM I'''
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===THE RECEPTOR-BINDING PROTEIN P2 OF BACTERIOPHAGE PRD1: CRYSTAL FORM I===
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==Overview==
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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 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.
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The line below this paragraph, {{ABSTRACT_PUBMED_12623018}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 12623018 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12623018}}
==About this Structure==
==About this Structure==
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[[Category: Proline-rich]]
[[Category: Proline-rich]]
[[Category: Viral receptor-binding]]
[[Category: Viral receptor-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:12:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:55:26 2008''

Revision as of 14:55, 27 July 2008

Image:1n7u.png

Template:STRUCTURE 1n7u

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

Template:ABSTRACT PUBMED 12623018

About this Structure

1N7U is a Single protein structure of sequence from Enterobacteria phage prd1. 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

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