4ITV

Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains, triple mutant, P212121 form

Summary for 4ITV

• Entry DOI: 10.2210/pdb4itv/pdb
• Related: 3VDX 4D9J 4IQ4 4IVJ
• Descriptor: Non-haem bromoperoxidase BPO-A2, Matrix protein 1 (1 entity in total)
• Functional Keywords: protein design, bionanotechnology, protein assembly, symmetric oligomeric domains, biomaterials, oxidoreductase
• Biological source: Streptomyces aureofaciens; More
• Cellular location: Virion membrane ; Peripheral membrane protein ; Cytoplasmic side : P03485
• Total number of polymer chains: 12
• Total formula weight: 603376.31

Authors

Lai, Y.-T.,Sawaya, M.R.,Yeates, T.O. (deposition date: 2013-01-18, release date: 2013-07-24, Last modification date: 2023-09-20)

Primary citation

Lai, Y.T.,Tsai, K.L.,Sawaya, M.R.,Asturias, F.J.,Yeates, T.O.
Structure and flexibility of nanoscale protein cages designed by symmetric self-assembly.
J.Am.Chem.Soc., 135:7738-7743, 2013

PubMed Abstract: Designing protein molecules that self-assemble into complex architectures is an outstanding goal in the area of nanobiotechnology. One design strategy for doing this involves genetically fusing together two natural proteins, each of which is known to form a simple oligomer on its own (e.g., a dimer or trimer). If two such components can be fused in a geometrically predefined configuration, that designed subunit can, in principle, assemble into highly symmetric architectures. Initial experiments showed that a 12-subunit tetrahedral cage, 16 nm in diameter, could be constructed following such a procedure [Padilla, J. E.; et al. Proc. Natl. Acad. Sci. U.S.A. 2001, 98, 2217; Lai, Y. T.; et al. Science 2012, 336, 1129]. Here we characterize multiple crystal structures of protein cages constructed in this way, including cages assembled from two mutant forms of the same basic protein subunit. The flexibilities of the designed assemblies and their deviations from the target model are described, along with implications for further design developments.

PubMed: 23621606
DOI: 10.1021/ja402277f

Experimental method

X-RAY DIFFRACTION (3.598 Å)