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 13.3Å" /> '''QUASI-ATOMIC RESOLUT...)
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Revision as of 14:12, 20 November 2007
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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
Page seeded by OCA on Tue Nov 20 16:19:14 2007
