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: 2024-05-01)

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 Abstract: Some capsid proteins built on the ubiquitous HK97-fold have accessory domains imparting specific functions. Bacteriophage P22 coat protein has a unique insertion domain (I-domain). Two prior I-domain models from subnanometer cryoelectron microscopy (cryoEM) reconstructions differed substantially. Therefore, the I-domain's nuclear magnetic resonance structure was determined and also used to improve cryoEM models of coat protein. The I-domain has an antiparallel six-stranded β-barrel fold, not previously observed in HK97-fold accessory domains. The D-loop, which is dynamic in the isolated I-domain and intact monomeric coat protein, forms stabilizing salt bridges between adjacent capsomers in procapsids. The S-loop is important for capsid size determination, likely through intrasubunit interactions. Ten of 18 coat protein temperature-sensitive-folding substitutions are in the I-domain, indicating its importance in folding and stability. Several are found on a positively charged face of the β-barrel that anchors the I-domain to a negatively charged surface of the coat protein HK97-core.

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

Experimental method

SOLUTION NMR