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Article: Hierarchical and helical self-assembly of ADP-ribosyl cyclase into large-scale protein microtubes

TitleHierarchical and helical self-assembly of ADP-ribosyl cyclase into large-scale protein microtubes
Authors
Issue Date2008
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jpcbfk
Citation
Journal Of Physical Chemistry B, 2008, v. 112 n. 47, p. 14682-14686 How to Cite?
AbstractProteins are macromolecules with characteristic structures and biological functions. It is extremely challenging to obtain protein microtube structures through self-assembly as proteins are very complex and flexible. Here we present a strategy showing how a specific protein, ADP-ribosyl cyclase, helically self-assembles from monomers into hexagonal nanochains and further to highly ordered crystalline microtubes. The structures of protein nanochains and consequently self-assembled superlattice were determined by X-ray crystallography at 4.5 Å resolution and imaged by scanning electron microscopy. The protein initially forms into dimers that have a fixed size of 5.6 nm, and then, helically self-assembles into 35.6 nm long hexagonal nanochains. One such nanochain consists of six dimers (12 monomers) that stack in order by a pseudo P6 1 screw axis. Seven nanochains produce a series of large-scale assemblies, nanorods, forming the building blocks for microrods. A proposed aging process of microrods results in the formation of hollow microstructures. Synthesis and characterization of large scale self-assembled protein microtubes may pave a new pathway, capable of not only understanding the self-assembly dynamics of biological materials, but also directing design and fabrication of multifunctional nanobuilding blocks with particular applications in biomedical engineering. © 2008 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/91908
ISSN
2015 Impact Factor: 3.187
2015 SCImago Journal Rankings: 1.414
ISI Accession Number ID
Funding AgencyGrant Number
NIHRR01646
GM061568
NSF
NIH National Institute of General Medical SciencesDMR-0225180
Funding Information:

We are grateful to Dr. Marian Szebenyi for help in the indexing of diffraction data and Professor Dan Luo and Professor Younan Xia for critical reading of the manuscript. SEM images were collected at the Cornell Integrated Microscopy Center (CIMC) with help from Drs. Mandayarn Parthasarathy and Carole Daugherty. This work was supported by grants from the NIH to MacCHESS (RR01646) and H.C.L./ Q.H. (GM061568). The crystallographic data were collected at the Cornell High Energy Synchrotron Source (CHESS), which is supported by the NSF and NIH National Institute of General Medical Sciences under award DMR-0225180.

References

 

DC FieldValueLanguage
dc.contributor.authorLiu, Qen_HK
dc.contributor.authorKriksunov, IAen_HK
dc.contributor.authorWang, Zen_HK
dc.contributor.authorGraeff, Ren_HK
dc.contributor.authorLee, HCen_HK
dc.contributor.authorHao, Qen_HK
dc.date.accessioned2010-09-17T10:30:12Z-
dc.date.available2010-09-17T10:30:12Z-
dc.date.issued2008en_HK
dc.identifier.citationJournal Of Physical Chemistry B, 2008, v. 112 n. 47, p. 14682-14686en_HK
dc.identifier.issn1520-6106en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91908-
dc.description.abstractProteins are macromolecules with characteristic structures and biological functions. It is extremely challenging to obtain protein microtube structures through self-assembly as proteins are very complex and flexible. Here we present a strategy showing how a specific protein, ADP-ribosyl cyclase, helically self-assembles from monomers into hexagonal nanochains and further to highly ordered crystalline microtubes. The structures of protein nanochains and consequently self-assembled superlattice were determined by X-ray crystallography at 4.5 Å resolution and imaged by scanning electron microscopy. The protein initially forms into dimers that have a fixed size of 5.6 nm, and then, helically self-assembles into 35.6 nm long hexagonal nanochains. One such nanochain consists of six dimers (12 monomers) that stack in order by a pseudo P6 1 screw axis. Seven nanochains produce a series of large-scale assemblies, nanorods, forming the building blocks for microrods. A proposed aging process of microrods results in the formation of hollow microstructures. Synthesis and characterization of large scale self-assembled protein microtubes may pave a new pathway, capable of not only understanding the self-assembly dynamics of biological materials, but also directing design and fabrication of multifunctional nanobuilding blocks with particular applications in biomedical engineering. © 2008 American Chemical Society.en_HK
dc.languageengen_HK
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jpcbfken_HK
dc.relation.ispartofJournal of Physical Chemistry Ben_HK
dc.titleHierarchical and helical self-assembly of ADP-ribosyl cyclase into large-scale protein microtubesen_HK
dc.typeArticleen_HK
dc.identifier.emailGraeff, R: graeffr@hku.hken_HK
dc.identifier.emailLee, HC: leehc@hku.hken_HK
dc.identifier.emailHao, Q: qhao@hku.hken_HK
dc.identifier.authorityGraeff, R=rp01464en_HK
dc.identifier.authorityLee, HC=rp00545en_HK
dc.identifier.authorityHao, Q=rp01332en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1021/jp807990gen_HK
dc.identifier.pmid18956900-
dc.identifier.scopuseid_2-s2.0-57449083063en_HK
dc.identifier.hkuros154345en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-57449083063&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume112en_HK
dc.identifier.issue47en_HK
dc.identifier.spage14682en_HK
dc.identifier.epage14686en_HK
dc.identifier.isiWOS:000261056400003-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLiu, Q=35215401600en_HK
dc.identifier.scopusauthoridKriksunov, IA=6507909504en_HK
dc.identifier.scopusauthoridWang, Z=36543473300en_HK
dc.identifier.scopusauthoridGraeff, R=7003614053en_HK
dc.identifier.scopusauthoridLee, HC=26642959100en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK

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