1GAV

BACTERIOPHAGE GA PROTEIN CAPSID

Summary for 1GAV

• Entry DOI: 10.2210/pdb1gav/pdb
• Descriptor: BACTERIOPHAGE GA PROTEIN CAPSID (1 entity in total)
• Functional Keywords: bacteriophage, capsid, coat protein, icosahedral virus, virus
• Biological source: Enterobacteria phage GA
• Total number of polymer chains: 45
• Total formula weight: 613592.32

Authors

Tars, K.,Bundule, M.,Liljas, L. (deposition date: 1997-01-28, release date: 1997-09-04, Last modification date: 2024-02-07)

Primary citation

Tars, K.,Bundule, M.,Fridborg, K.,Liljas, L.
The crystal structure of bacteriophage GA and a comparison of bacteriophages belonging to the major groups of Escherichia coli leviviruses.
J.Mol.Biol., 271:759-773, 1997

PubMed Abstract: The three-dimensional structure of the small T=3 RNA bacteriophage GA has been determined at 3.4 A resolution. The structure was solved by molecular replacement, using the phage MS2 as an initial model. A comparison of the protein shells of the four related phages GA, MS2, fr and Qbeta was carried out in order to define structural features of particular importance for their assembly and specific RNA interaction. A high degree of similarity was found in the RNA binding sites, whereas larger structural differences are located in the loop regions of the coat proteins, especially in the FG loops forming 5-fold and quasi-6-fold contacts. The overall arrangement of the protein subunits in the shells of these phages is very similar, although the details of the interactions differ. The few conserved interactions are suggested to govern the subunit packing during assembly.

PubMed: 9299325
DOI: 10.1006/jmbi.1997.1214

Experimental method

X-RAY DIFFRACTION (3.4 Å)