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; PubMed: 24836025; DOI: 10.1016/j.str.2014.04.003

Experimental method

SOLUTION NMR