2bpa
From Proteopedia
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ATOMIC STRUCTURE OF SINGLE-STRANDED DNA BACTERIOPHAGE PHIX174 AND ITS FUNCTIONAL IMPLICATIONS
Overview
The mechanism of DNA ejection, viral assembly and evolution are related to, the structure of bacteriophage phi X174. The F protein forms a T = 1, capsid whose major folding motif is the eight-stranded antiparallel beta, barrel found in many other icosahedral viruses. Groups of 5 G proteins, form 12 dominating spikes that enclose a hydrophilic channel containing, some diffuse electron density. Each G protein is a tight beta barrel with, its strands running radially outwards and with a topology similar to that, of the F protein. The 12 'pilot' H proteins per virion may be partially, located in the putative ion channel. The small, basic J protein is, associated with the DNA and is situated in an interior cleft of the F, protein. Tentatively, there are three regions of partially ordered DNA, structure,
About this Structure
2BPA is a Protein complex structure of sequences from Enterobacteria phage phix174. Full crystallographic information is available from OCA.
Reference
Atomic structure of single-stranded DNA bacteriophage phi X174 and its functional implications., McKenna R, Xia D, Willingmann P, Ilag LL, Krishnaswamy S, Rossmann MG, Olson NH, Baker TS, Incardona NL, Nature. 1992 Jan 9;355(6356):137-43. PMID:1370343
Page seeded by OCA on Wed Nov 21 08:51:54 2007
