1gw7: Difference between revisions

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[[Image:1gw7.~~gif~~|left|200px]]

[[Image:1gw7.png|left|200px]]

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~~'''~~QUASI-ATOMIC RESOLUTION MODEL OF BACTERIOPHAGE PRD1 CAPSID, OBTAINED BY COMBINED CRYO-EM AND X-RAY CRYSTALLOGRAPHY.~~'''~~

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

~~==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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_12219080}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12219080 is the PubMed ID number.

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==About this Structure==

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[[Category: Tectiviridae]]

[[Category: Virus/viral protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 18~~:05:19 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:12:15 2008''

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-[[Image:1gw7.gif|left|200px]]
+{{Seed}}
+[[Image:1gw7.png|left|200px]]
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 {{STRUCTURE_1gw7|  PDB=1gw7  |  SCENE=  }}
-'''QUASI-ATOMIC RESOLUTION MODEL OF BACTERIOPHAGE PRD1 CAPSID, OBTAINED BY COMBINED CRYO-EM AND X-RAY CRYSTALLOGRAPHY.'''
+===QUASI-ATOMIC RESOLUTION MODEL OF BACTERIOPHAGE PRD1 CAPSID, 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12219080}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12219080 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12219080}}
 ==About this Structure==
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 [[Category: Tectiviridae]]
 [[Category: Virus/viral protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:05:19 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 06:12:15 2008''