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 2.40&Aring;" /> '''THE RECEPTOR-BINDING...)
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[[Image:1n7u.jpg|left|200px]]<br /><applet load="1n7u" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1n7u.jpg|left|200px]]<br /><applet load="1n7u" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1n7u, resolution 2.40&Aring;" />
caption="1n7u, resolution 2.40&Aring;" />
'''THE RECEPTOR-BINDING PROTEIN P2 OF BACTERIOPHAGE PRD1: CRYSTAL FORM I'''<br />
'''THE RECEPTOR-BINDING PROTEIN P2 OF BACTERIOPHAGE PRD1: CRYSTAL FORM I'''<br />
==Overview==
==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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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==
==About this Structure==
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1N7U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_prd1 Enterobacteria phage prd1] with ACT and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N7U OCA].
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1N7U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_prd1 Enterobacteria phage prd1] with <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N7U OCA].
==Reference==
==Reference==
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[[Category: Enterobacteria phage prd1]]
[[Category: Enterobacteria phage prd1]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bamford, D.H.]]
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[[Category: Bamford, D H.]]
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[[Category: Benson, S.D.]]
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[[Category: Benson, S D.]]
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[[Category: Burnett, R.M.]]
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[[Category: Burnett, R M.]]
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[[Category: Butcher, S.J.]]
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[[Category: Butcher, S J.]]
[[Category: Xu, L.]]
[[Category: Xu, L.]]
[[Category: ACT]]
[[Category: ACT]]
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[[Category: viral receptor-binding]]
[[Category: viral receptor-binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:01:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:03:15 2008''

Revision as of 12:03, 21 February 2008


1n7u, resolution 2.40Å

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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 and 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

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