Structure of a 16-nm Cage Designed by Using Protein Oligomers

Designing protein molecules that will assemble into various kinds of ordered materials represents an important challenge in nanotechnology. We report the crystal structure of a 12-subunit protein cage that self-assembles by design to form a tetrahedral structure roughly 16 nanometers in diameter. Th...

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Veröffentlicht in:	Science (American Association for the Advancement of Science) 2012-06, Vol.336 (6085), p.1129-1129
Hauptverfasser:	Lai, Yen-Ting, Cascio, Duilio, Yeates, Todd O.
Format:	Artikel
Sprache:	eng
Schlagworte:	60 APPLIED LIFE SCIENCES Architecture (computers) Atomic structure BASIC BIOLOGICAL SCIENCES Binding Binding sites Biological and medical sciences BREVIA Cage Construction CRYSTAL STRUCTURE Crystalline structure Crystallography, X-Ray DESIGN Fundamental and applied biological sciences. Psychology Geometry Interfaces Materials Models, Molecular Molecular biophysics Molecular structure Molecules Oligomers Peroxidases - chemistry Protein Conformation Protein Engineering Protein Multimerization Protein Structure, Secondary Protein Structure, Tertiary Protein Subunits - chemistry PROTEINS Proteins - chemistry Self assembly Structure in molecular biology Symmetry Viral Matrix Proteins - chemistry
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Zusammenfassung:	Designing protein molecules that will assemble into various kinds of ordered materials represents an important challenge in nanotechnology. We report the crystal structure of a 12-subunit protein cage that self-assembles by design to form a tetrahedral structure roughly 16 nanometers in diameter. The strategy of fusing together oligomeric protein domains can be generalized to produce other kinds of cages or extended materials.
ISSN:	0036-8075 1095-9203
DOI:	10.1126/science.1219351