4Y4Y

T=1 capsid structure of SeMV Ndel65CP fused with B-domain of S. aureus protein SpA at the N-terminus (C2 crystal form)

Summary for 4Y4Y

• Entry DOI: 10.2210/pdb4y4y/pdb
• Related: 1VAK
• Descriptor: Immunoglobulin G-binding protein A,Coat protein, SULFATE ION (3 entities in total)
• Functional Keywords: coat protein, chimeric vlp, in vitro assembly, virus
• Biological source: Staphylococcus aureus; More
• Total number of polymer chains: 30
• Total formula weight: 916872.77

Authors

Gulati, A.,Murthy, M.R.N. (deposition date: 2015-02-11, release date: 2016-01-20, Last modification date: 2024-10-23)

Primary citation

Gulati, A.,Murthy, A.,Abraham, A.,Mohan, K.,Natraj, U.,Savithri, H.S.,Murthy, M.R.
Structural studies on chimeric Sesbania mosaic virus coat protein: Revisiting SeMV assembly.
Virology, 489:34-43, 2015

PubMed Abstract: The capsid protein (CP) of Sesbania mosaic virus (SeMV, a T=3 plant virus) consists of a disordered N-terminal R-domain and an ordered S-domain. Removal of the R-domain results in the formation of T=1 particles. In the current study, the R-domain was replaced with unrelated polypeptides of similar lengths: the B-domain of Staphylococcus aureus SpA, and SeMV encoded polypeptides P8 and P10. The chimeric proteins contained T=3 or larger virus-like particles (VLPs) and could not be crystallized. The presence of metal ions during purification resulted in a large number of heterogeneous nucleoprotein complexes. N∆65-B (R domain replaced with B domain) could also be purified in a dimeric form. Its crystal structure revealed T=1 particles devoid of metal ions and the B-domain was disordered. However, the B-domain was functional in N∆65-B VLPs, suggesting possible biotechnological applications. These studies illustrate the importance of N-terminal residues, metal ions and robustness of the assembly process.

PubMed: 26704627
DOI: 10.1016/j.virol.2015.11.029

Experimental method

X-RAY DIFFRACTION (3 Å)