Biswas, S and Garg, P and Dutta, S and Suguna, K (2021) Multiple nanocages of a cyanophage small heat shock protein with icosahedral and octahedral symmetries. In: Scientific Reports, 11 (1).
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Abstract
The structures of a cyanophage small heat shock protein (sHSP) were determined as octahedrons of 24-mers and 48-mers and as icosahedrons of 60-mers. An N-terminal deletion construct of an 18 kDa sHSP of Synechococcus sp. phage S-ShM2 crystallized as a 24-mer and its structure was determined at a resolution of 7 Å. The negative stain electron microscopy (EM) images showed that the full-length protein is a mixture of a major population of larger and a minor population of smaller cage-like particles. Their structures have been determined by electron cryomicroscopy 3D image reconstruction at a resolution of 8 Å. The larger particles are 60-mers with icosahedral symmetry and the smaller ones are 48-mers with octahedral symmetry. These structures are the first of the viral/phage origin and the 60-mer is the largest and the first icosahedral assembly to be reported for sHSPs.
| Item Type: | Journal Article |
|---|---|
| Publication: | Scientific Reports |
| Publisher: | Nature Research |
| Additional Information: | The copyright for this article belongs to the Authors. |
| Keywords: | Amino Acid Sequence; Bacteriophages; Conserved Sequence; Cryoelectron Microscopy; Heat-Shock Proteins, Small; Models, Molecular; Molecular Chaperones; Molecular Weight; Mutation; Protein Aggregates; Protein Binding; Protein Conformation; Protein Multimerization; Structure-Activity Relationship; Viral Proteins chaperone; protein aggregate; protein binding; small heat shock protein; viral protein, amino acid sequence; bacteriophage; chemistry; conserved sequence; cryoelectron microscopy; genetics; metabolism; molecular model; molecular weight; mutation; protein conformation; protein multimerization; structure activity relation, Amino Acid Sequence; Bacteriophages; Conserved Sequence; Cryoelectron Microscopy; Heat-Shock Proteins, Small; Models, Molecular; Molecular Chaperones; Molecular Weight; Mutation; Protein Aggregates; Protein Binding; Protein Conformation; Protein Multimerization; Structure-Activity Relationship; Viral Proteins amino acid sequence; bacteriophage; chemistry; conserved sequence; cryoelectron microscopy; genetics; metabolism; molecular model; molecular weight; mutation; protein conformation; protein multimerization; structure activity relation |
| Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit Division of Physical & Mathematical Sciences > Physics |
| Date Deposited: | 09 Jun 2023 10:46 |
| Last Modified: | 09 Jun 2023 10:46 |
| URI: | https://eprints.iisc.ac.in/id/eprint/81837 |
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