1FRS

CRYSTAL STRUCTURE OF BACTERIOPHAGE FR CAPSIDS AT 3.5 ANGSTROMS RESOLUTION

Summary for 1FRS

• Entry DOI: 10.2210/pdb1frs/pdb
• Descriptor: BACTERIOPHAGE FR CAPSID (1 entity in total)
• Functional Keywords: coat protein (viral), icosahedral virus, virus
• Biological source: Enterobacteria phage fr
• Total number of polymer chains: 3
• Total formula weight: 41239.27

Authors

Liljas, L.,Valegard, K.,Bundule, M. (deposition date: 1994-08-16, release date: 1996-04-03, Last modification date: 2024-05-22)

Primary citation

Liljas, L.,Fridborg, K.,Valegard, K.,Bundule, M.,Pumpens, P.
Crystal structure of bacteriophage fr capsids at 3.5 A resolution.
J.Mol.Biol., 244:279-290, 1994

PubMed Abstract: The structure of recombinant capsids of the bacterial virus fr has been determined by X-ray crystallography at 3.5 A resolution. The capsids were produced by expressing the fr coat protein in Escherichia coli, the natural host of the virus, and are probably essentially identical to the protein shell of the native virus. The structure was determined using molecular replacement with the protein shell of the related MS2 virus, and refined to a crystallographic R-factor of 0.228. A comparison of the protein shells of the viruses shows that they are very similar, and indicates that they may have a similar regulation of the assembly of the quasi-symmetrical protein shell.

PubMed: 7966339
DOI: 10.1006/jmbi.1994.1729

Experimental method

X-RAY DIFFRACTION (3.5 Å)