GSTDTAP  > 地球科学
DOI10.1038/s41586-019-1928-2
Constructing protein polyhedra via orthogonal chemical interactions
Mooley, K. P.; Deller, A. T.; Gottlieb, O.; Nakar, E.; Hallinan, G.; Bourke, S.; Frail, D. A.; Horesh, A.; Corsi, A.; Hotokezaka, K.
2020-01-09
发表期刊NATURE
ISSN0028-0836
EISSN1476-4687
出版年2020
卷号578期号:7793页码:172-+
文章类型Article
语种英语
国家USA
英文关键词

Many proteins exist naturally as symmetrical homooligomers or homopolymers(1). The emergent structural and functional properties of such protein assemblies have inspired extensive efforts in biomolecular design(2-5). As synthesized by ribosomes, proteins are inherently asymmetric. Thus, they must acquire multiple surface patches that selectively associate to generate the different symmetry elements needed to form higher-order architectures(1,6)-a daunting task for protein design. Here we address this problem using an inorganic chemical approach, whereby multiple modes of protein-protein interactions and symmetry are simultaneously achieved by selective, ' one-pot' coordination of soft and hard metal ions. We show that a monomeric protein (protomer) appropriately modified with biologically inspired hydroxamate groups and zinc-binding motifs assembles through concurrent Fe3+ and Zn2+ coordination into discrete dodecameric and hexameric cages. Our cages closely resemble natural polyhedral protein architectures(7,8) and are, to our knowledge, unique among designed systems(9-13) in that they possess tightly packed shells devoid of large apertures. At the same time, they can assemble and disassemble in response to diverse stimuli, owing to their heterobimetallic construction on minimal interprotein-bonding footprints. With stoichiometries ranging from [2 Fe:9 Zn:6 protomers] to [8 Fe:21 Zn:12 protomers], these protein cages represent some of the compositionally most complex protein assemblies-or inorganic coordination complexes-obtained by design.


An inorganic chemical approach to biomolecular design is used to generate ' cages' that can simultaneously promote symmetry and multiple modes of protein interactions.


领域地球科学 ; 气候变化 ; 资源环境
收录类别SCI-E
WOS记录号WOS:000508801100003
WOS关键词COORDINATION CHEMISTRY ; DESIGN ; CRYSTAL ; CAGES ; VISUALIZATION ; STABILITY ; DYNAMICS ; SYMMETRY ; MODEL
WOS类目Multidisciplinary Sciences
WOS研究方向Science & Technology - Other Topics
引用统计
文献类型期刊论文
条目标识符http://119.78.100.173/C666/handle/2XK7JSWQ/281441
专题地球科学
资源环境科学
气候变化
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GB/T 7714
Mooley, K. P.,Deller, A. T.,Gottlieb, O.,et al. Constructing protein polyhedra via orthogonal chemical interactions[J]. NATURE,2020,578(7793):172-+.
APA Mooley, K. P..,Deller, A. T..,Gottlieb, O..,Nakar, E..,Hallinan, G..,...&Hotokezaka, K..(2020).Constructing protein polyhedra via orthogonal chemical interactions.NATURE,578(7793),172-+.
MLA Mooley, K. P.,et al."Constructing protein polyhedra via orthogonal chemical interactions".NATURE 578.7793(2020):172-+.
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