2M5S
High-resolution NMR structure and cryo-EM imaging support multiple functional roles for the accessory I-domain of phage P22 coat protein
Summary for 2M5S
Entry DOI | 10.2210/pdb2m5s/pdb |
Related | 2XYY 2XYZ 3IYH 3IYI |
NMR Information | BMRB: 18566 |
Descriptor | Coat protein (1 entity in total) |
Functional Keywords | telokin-like domain, extra-density domain, d-loop, viral protein |
Biological source | Enterobacteria phage P22 |
Cellular location | Virion (Potential): P26747 |
Total number of polymer chains | 1 |
Total formula weight | 13865.56 |
Authors | Rizzo, A.A.,Suhanovsky, M.M.,Baker, M.L.,Fraser, L.C.R.,Jones, L.M.,Rempel, D.L.,Gross, M.L.,Chiu, W.,Alexandrescu, A.T.,Teschke, C.M. (deposition date: 2013-03-05, release date: 2014-03-05, Last modification date: 2014-07-02) |
Primary citation | Rizzo, A.A.,Suhanovsky, M.M.,Baker, M.L.,Fraser, L.C.,Jones, L.M.,Rempel, D.L.,Gross, M.L.,Chiu, W.,Alexandrescu, A.T.,Teschke, C.M. Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling. Structure, 22:830-841, 2014 Cited by PubMed: 24836025DOI: 10.1016/j.str.2014.04.003 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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