4BML
C-alpha backbone trace of major capsid protein gp39 found in marine virus Syn5.
Summary for 4BML
| Entry DOI | 10.2210/pdb4bml/pdb |
| EMDB information | 5954 |
| Descriptor | MAJOR CAPSID PROTEIN (1 entity in total) |
| Functional Keywords | virus, marine virus, outer capsid protein, maturation |
| Biological source | SYNECHOCOCCUS PHAGE SYN5 (HORNED VIRUS SYN5) |
| Total number of polymer chains | 7 |
| Total formula weight | 245741.86 |
| Authors | Gipson, P.,Baker, M.L.,Raytcheva, D.,Haase-Pettingell, C.,Piret, J.,King, J.,Chiu, W. (deposition date: 2013-05-09, release date: 2014-05-21, Last modification date: 2024-05-08) |
| Primary citation | Gipson, P.,Baker, M.L.,Raytcheva, D.,Haase-Pettingell, C.,Piret, J.,King, J.A.,Chiu, W. Protruding Knob-Like Proteins Violate Local Symmetries in an Icosahedral Marine Virus. Nat.Commun., 5:4278-, 2014 Cited by PubMed Abstract: Marine viruses play crucial roles in shaping the dynamics of oceanic microbial communities and in the carbon cycle on Earth. Here we report a 4.7-Å structure of a cyanobacterial virus, Syn5, by electron cryo-microscopy and modelling. A Cα backbone trace of the major capsid protein (gp39) reveals a classic phage protein fold. In addition, two knob-like proteins protruding from the capsid surface are also observed. Using bioinformatics and structure analysis tools, these proteins are identified to correspond to gp55 and gp58 (each with two copies per asymmetric unit). The non 1:1 stoichiometric distribution of gp55/58 to gp39 breaks all expected local symmetries and leads to non-quasi-equivalence of the capsid subunits, suggesting a role in capsid stabilization. Such a structural arrangement has not yet been observed in any known virus structures. PubMed: 24985522DOI: 10.1038/NCOMMS5278 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.7 Å) |
Structure validation
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