1gw8

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(New page: 200px<br /><applet load="1gw8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gw8, resolution 13.3&Aring;" /> '''QUASI-ATOMIC RESOLUT...)
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[[Image:1gw8.gif|left|200px]]<br /><applet load="1gw8" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1gw8.gif|left|200px]]<br /><applet load="1gw8" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1gw8, resolution 13.3&Aring;" />
caption="1gw8, resolution 13.3&Aring;" />
'''QUASI-ATOMIC RESOLUTION MODEL OF BACTERIOPHAGE PRD1 SUS607 MUTANT, OBTAINED BY COMBINED CRYO-EM AND X-RAY CRYSTALLOGRAPHY.'''<br />
'''QUASI-ATOMIC RESOLUTION MODEL OF BACTERIOPHAGE PRD1 SUS607 MUTANT, OBTAINED BY COMBINED CRYO-EM AND X-RAY CRYSTALLOGRAPHY.'''<br />
==Overview==
==Overview==
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Bacteriophage PRD1 shares many structural and functional similarities with, adenovirus. A major difference is the PRD1 internal membrane, which acts, in concert with vertex proteins to translocate the phage genome into the, host. Multiresolution models of the PRD1 capsid, together with genetic, analyses, provide fine details of the molecular interactions associated, with particle stability and membrane dynamics. The N- and C-termini of the, major coat protein (P3), which are required for capsid assembly, act as, conformational switches bridging capsid to membrane and linking P3, trimers. Electrostatic P3-membrane interactions increase virion stability, upon DNA packaging. Newly revealed proteins suggest how the metastable, vertex works and how the capsid edges are stabilized.
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Bacteriophage PRD1 shares many structural and functional similarities with adenovirus. A major difference is the PRD1 internal membrane, which acts in concert with vertex proteins to translocate the phage genome into the host. Multiresolution models of the PRD1 capsid, together with genetic analyses, provide fine details of the molecular interactions associated with particle stability and membrane dynamics. The N- and C-termini of the major coat protein (P3), which are required for capsid assembly, act as conformational switches bridging capsid to membrane and linking P3 trimers. Electrostatic P3-membrane interactions increase virion stability upon DNA packaging. Newly revealed proteins suggest how the metastable vertex works and how the capsid edges are stabilized.
==About this Structure==
==About this Structure==
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1GW8 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]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GW8 OCA].
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1GW8 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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GW8 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: Bamford, J.K.H.]]
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[[Category: Bamford, J K.H.]]
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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.]]
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[[Category: Fuller, S.D.]]
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[[Category: Fuller, S D.]]
[[Category: Huiskonen, J.]]
[[Category: Huiskonen, J.]]
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[[Category: Martin, C.San.]]
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[[Category: Martin, C San.]]
[[Category: bacteriophage prd1]]
[[Category: bacteriophage prd1]]
[[Category: cryo-em]]
[[Category: cryo-em]]
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[[Category: virus/viral protein]]
[[Category: virus/viral protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:19:14 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:54:37 2008''

Revision as of 10:54, 21 February 2008


1gw8, resolution 13.3Å

Drag the structure with the mouse to rotate

QUASI-ATOMIC RESOLUTION MODEL OF BACTERIOPHAGE PRD1 SUS607 MUTANT, OBTAINED BY COMBINED CRYO-EM AND X-RAY CRYSTALLOGRAPHY.

Overview

Bacteriophage PRD1 shares many structural and functional similarities with adenovirus. A major difference is the PRD1 internal membrane, which acts in concert with vertex proteins to translocate the phage genome into the host. Multiresolution models of the PRD1 capsid, together with genetic analyses, provide fine details of the molecular interactions associated with particle stability and membrane dynamics. The N- and C-termini of the major coat protein (P3), which are required for capsid assembly, act as conformational switches bridging capsid to membrane and linking P3 trimers. Electrostatic P3-membrane interactions increase virion stability upon DNA packaging. Newly revealed proteins suggest how the metastable vertex works and how the capsid edges are stabilized.

About this Structure

1GW8 is a Single protein structure of sequence from Enterobacteria phage prd1. Full crystallographic information is available from OCA.

Reference

Minor proteins, mobile arms and membrane-capsid interactions in the bacteriophage PRD1 capsid., San Martin C, Huiskonen JT, Bamford JK, Butcher SJ, Fuller SD, Bamford DH, Burnett RM, Nat Struct Biol. 2002 Oct;9(10):756-63. PMID:12219080

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