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Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domainsStructure of a 16 nm protein cage designed by fusing symmetric oligomeric domains
Structural highlights
Function[BPOA2_STRAU] May be a chlorinating enzyme involved in 7-chlorotetracycline biosynthesis. Publication Abstract from PubMedDesigning 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. Structure of a 16-nm cage designed by using protein oligomers.,Lai YT, Cascio D, Yeates TO Science. 2012 Jun 1;336(6085):1129. PMID:22654051[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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