Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling
| Autor: | LaTasha C.R. Fraser, Margaret M. Suhanovsky, Matthew L. Baker, Carolyn M. Teschke, Michael L. Gross, Wah Chiu, Don L. Rempel, Lisa M. Jones, Andrei T. Alexandrescu, Alessandro A. Rizzo |
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| Rok vydání: | 2014 |
| Předmět: |
Models
Molecular Viral protein Protein subunit Static Electricity Molecular Dynamics Simulation Antiparallel (biochemistry) medicine.disease_cause Article Bacteriophage 03 medical and health sciences Structural Biology Static electricity medicine Protein Structure Quaternary Nuclear Magnetic Resonance Biomolecular Molecular Biology Bacteriophage P22 030304 developmental biology 0303 health sciences biology Cryoelectron Microscopy 030302 biochemistry & molecular biology Capsomere biology.organism_classification Protein tertiary structure Protein Structure Tertiary Protein Subunits Crystallography Capsid Biophysics Capsid Proteins |
| Zdroj: | Structure. 22(6):830-841 |
| ISSN: | 0969-2126 |
| DOI: | 10.1016/j.str.2014.04.003 |
| Popis: | Summary 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. |
| Databáze: | OpenAIRE |
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