5FUA

Cryo-EM of BK polyomavirus

Summary for 5FUA

• Entry DOI: 10.2210/pdb5fua/pdb
• EMDB information: 3283
• Descriptor: MAJOR CAPSID PROTEIN VP1 (1 entity in total)
• Functional Keywords: virus, bkpyv, bk, polyomavirus
• Biological source: BK POLYOMAVIRUS
• Total number of polymer chains: 6
• Total formula weight: 240927.70

Authors

Hurdiss, D.L.,Morgan, E.L.,Thompson, R.F.,Prescott, E.L.,Panou, M.M.,Macdonald, A.,Ranson, N.A. (deposition date: 2016-01-22, release date: 2016-04-20, Last modification date: 2024-05-08)

Primary citation

Hurdiss, D.L.,Morgan, E.L.,Thompson, R.F.,Prescott, E.L.,Panou, M.M.,Macdonald, A.,Ranson, N.A.
New Structural Insights Into the Genome and Minor Capsid Proteins of Bk Polyomavirus Using Cryo-Electron Microscopy.
Structure, 24:528-, 2016

PubMed Abstract: BK polyomavirus is the causative agent of several diseases in transplant patients and the immunosuppressed. In order to better understand the structure and life cycle of BK, we produced infectious virions and VP1-only virus-like particles in cell culture, and determined their three-dimensional structures using cryo-electron microscopy (EM) and single-particle image processing. The resulting 7.6-Å resolution structure of BK and 9.1-Å resolution of the virus-like particles are the highest-resolution cryo-EM structures of any polyomavirus. These structures confirm that the architecture of the major structural protein components of these human polyomaviruses are similar to previous structures from other hosts, but give new insight into the location and role of the enigmatic minor structural proteins, VP2 and VP3. We also observe two shells of electron density, which we attribute to a structurally ordered part of the viral genome, and discrete contacts between this density and both VP1 and the minor capsid proteins.

PubMed: 26996963
DOI: 10.1016/J.STR.2016.02.008

Experimental method

ELECTRON MICROSCOPY (7.6 Å)