dc.contributor.authorPopp, David
dc.contributor.authorNarita, Akihiro
dc.contributor.authorLee, Lin Jie
dc.contributor.authorGhoshdastider, Umesh
dc.contributor.authorXue, Bo
dc.contributor.authorSrinivasan, Ramanujam
dc.contributor.authorBalasubramanian, Mohan K.
dc.contributor.authorTanaka, Toshitsugu
dc.contributor.authorRobinson, Robert C.
dc.date.accessioned2013-10-31T01:36:32Z
dc.date.available2013-10-31T01:36:32Z
dc.date.copyright2012en_US
dc.date.issued2012
dc.identifier.citationPopp, D., Narita, A., Lee, L. J., Ghoshdastider, U., Xue, B., Srinivasan, R., et al. (2012). Novel actin-like filament structure from Clostridium tetani. Journal of biological chemistry, 287(25), 21121-21129.en_US
dc.identifier.urihttp://hdl.handle.net/10220/17093
dc.description.abstractEukaryotic F-actin is constructed from two protofilaments that gently wind around each other to form a helical polymer. Several bacterial actin-like proteins (Alps) are also known to form F-actin-like helical arrangements from two protofilaments, yet with varied helical geometries. Here, we report a unique filament architecture of Alp12 from Clostridium tetani that is constructed from four protofilaments. Through fitting of an Alp12 monomer homology model into the electron microscopy data, the filament was determined to be constructed from two antiparallel strands, each composed of two parallel protofilaments. These four protofilaments form an open helical cylinder separated by a wide cleft. The molecular interactions within single protofilaments are similar to F-actin, yet interactions between protofilaments differ from those in F-actin. The filament structure and assembly and disassembly kinetics suggest Alp12 to be a dynamically unstable force-generating motor involved in segregating the pE88 plasmid, which encodes the lethal tetanus toxin, and thus a potential target for drug design. Alp12 can be repeatedly cycled between states of polymerization and dissociation, making it a novel candidate for incorporation into fuel-propelled nanobiopolymer machines.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesJournal of biological chemistryen_US
dc.rights© 2012 The American Society for Biochemistry and Molecular Biology, Inc.en_US
dc.subjectDRNTU::Science::Biological sciences
dc.titleNovel actin-like filament structure from Clostridium tetanien_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doihttp://dx.doi.org/10.1074/jbc.M112.341016


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