4ZOR
The structure of the S37P MS2 viral capsid assembly.
Summary for 4ZOR
Entry DOI | 10.2210/pdb4zor/pdb |
Descriptor | Coat protein, PHOSPHATE ION (3 entities in total) |
Functional Keywords | capsid, virus like particle, virus |
Biological source | Enterobacteria phage MS2 |
Cellular location | Virion : P03612 |
Total number of polymer chains | 5 |
Total formula weight | 69122.39 |
Authors | Asensio, M.A.,Sankaran, B.,Zwart, P.H.,Tullman-Ercek, D. (deposition date: 2015-05-06, release date: 2016-09-07, Last modification date: 2023-09-27) |
Primary citation | Asensio, M.A.,Morella, N.M.,Jakobson, C.M.,Hartman, E.C.,Glasgow, J.E.,Sankaran, B.,Zwart, P.H.,Tullman-Ercek, D. A Selection for Assembly Reveals That a Single Amino Acid Mutant of the Bacteriophage MS2 Coat Protein Forms a Smaller Virus-like Particle. Nano Lett., 16:5944-5950, 2016 Cited by PubMed Abstract: Virus-like particles are used to encapsulate drugs, imaging agents, enzymes, and other biologically active molecules in order to enhance their function. However, the size of most virus-like particles is inflexible, precluding the design of appropriately sized containers for different applications. Here, we describe a chromatographic selection for virus-like particle assembly. Using this selection, we identified a single amino acid substitution to the coat protein of bacteriophage MS2 that mediates a uniform switch in particle geometry from T = 3 to T = 1 icosahedral symmetry. The resulting smaller particle retains the ability to be disassembled and reassembled in vitro and to be chemically modified to load cargo into its interior cavity. The pair of 27 and 17 nm MS2 particles will allow direct examination of the effect of size on function in established applications of virus-like particles, including drug delivery and imaging. PubMed: 27549001DOI: 10.1021/acs.nanolett.6b02948 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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