2VVF

Crystal structure of the major capsid protein P2 from Bacteriophage PM2

Summary for 2VVF

• Entry DOI: 10.2210/pdb2vvf/pdb
• Descriptor: MAJOR CAPSID PROTEIN P2, CALCIUM ION (3 entities in total)
• Functional Keywords: double jelly-roll viral capsid, viral protein
• Biological source: PSEUDOALTEROMONAS PHAGE PM2 (PM2)
• Total number of polymer chains: 6
• Total formula weight: 181642.81

Authors

Abrescia, N.G.A.,Grimes, J.M.,Kivela, H.K.,Assenberg, R.,Sutton, G.C.,Butcher, S.J.,Bamford, J.K.H.,Bamford, D.H.,Stuart, D.I. (deposition date: 2008-06-06, release date: 2008-09-16, Last modification date: 2024-05-08)

Primary citation

Abrescia, N.G.A.,Grimes, J.M.,Kivela, H.K.,Assenberg, R.,Sutton, G.C.,Butcher, S.J.,Bamford, J.K.H.,Bamford, D.H.,Stuart, D.I.
Insights Into Virus Evolution and Membrane Biogenesis from the Structure of the Marine Lipid-Containing Bacteriophage Pm2.
Mol.Cell, 31:749-, 2008

PubMed Abstract: Recent, primarily structural observations indicate that related viruses, harboring no sequence similarity, infect hosts of different domains of life. One such clade of viruses, defined by common capsid architecture and coat protein fold, is the so-called PRD1-adenovirus lineage. Here we report the structure of the marine lipid-containing bacteriophage PM2 determined by crystallographic analyses of the entire approximately 45 MDa virion and of the outer coat proteins P1 and P2, revealing PM2 to be a primeval member of the PRD1-adenovirus lineage with an icosahedral shell and canonical double beta barrel major coat protein. The view of the lipid bilayer, richly decorated with membrane proteins, constitutes a rare visualization of an in vivo membrane. The viral membrane proteins P3 and P6 are organized into a lattice, suggesting a possible assembly pathway to produce the mature virus.

PubMed: 18775333
DOI: 10.1016/J.MOLCEL.2008.06.026

Experimental method

X-RAY DIFFRACTION (2.5 Å)