dc.contributor.authorLim, Jackwee
dc.contributor.authorSun, Huihua
dc.contributor.authorFan, Jing-Song
dc.contributor.authorHameed, Iman Fahim
dc.contributor.authorLescar, Julien
dc.contributor.authorLiang, Zhao-Xun
dc.contributor.authorYang, Daiwen
dc.date.accessioned2013-06-27T04:02:17Z
dc.date.available2013-06-27T04:02:17Z
dc.date.copyright2012en_US
dc.date.issued2012
dc.identifier.citationLim, J., Sun, H., Fan, J.-S., Hameed, I. F., Lescar, J., Liang, Z.-X., et al. (2012). Rigidifying Acyl Carrier Protein Domain in Iterative Type I PKS CalE8 Does Not Affect Its Function. Biophysical Journal, 103(5), 1037-1044.en_US
dc.identifier.issn0006-3495en_US
dc.identifier.urihttp://hdl.handle.net/10220/10787
dc.description.abstractAcyl carrier protein (ACP) domains shuttle acyl intermediates among the catalytic domains of multidomain type I fatty acid synthase and polyketide synthase (PKS) systems. It is believed that the unique function of ACPs is associated with their dynamic property, but it remains to be fully elucidated what type of protein dynamics is critical for the shuttling domain. Using NMR techniques, we found that the ACP domain of iterative type I PKS CalE8 from Micromonospora echinospora is highly dynamic on the millisecond-second timescale. Introduction of an interhelical disulfide linkage in the ACP domain suppresses the dynamics on the millisecond-second timescale and reduces the mobility on the picosecond-nanosecond timescale. We demonstrate that the full-length PKS is fully functional upon rigidification of the ACP domain, suggesting that although the flexibility of the disordered terminal linkers may be important for the function of the ACP domain, the internal dynamics of the helical regions is not critical for that function.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesBiophysical journalen_US
dc.rights© 2012 The Biophysical Society.en_US
dc.subjectDRNTU::Science::Biological sciences
dc.titleRigidifying acyl carrier protein domain in iterative type I PKS CalE8 does not affect its functionen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doihttp://dx.doi.org/10.1016/j.bpj.2012.08.006


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