Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/139321
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dc.contributor.authorKamariah, Neelagandanen_US
dc.contributor.authorHuber, Roland G.en_US
dc.contributor.authorNartey, Wilsonen_US
dc.contributor.authorBhushan, Shashien_US
dc.contributor.authorBond, Peter J.en_US
dc.contributor.authorGrüber, Gerharden_US
dc.date.accessioned2020-05-19T01:17:30Z-
dc.date.available2020-05-19T01:17:30Z-
dc.date.issued2019-
dc.identifier.citationKamariah, N., Huber, R. G., Nartey, W., Bhushan, S., Bond, P. J., & Grüber, G. (2019). Structure and subunit arrangement of Mycobacterial F1FO ATP synthase and novel features of the unique mycobacterial subunit δ. Journal of Structural Biology, 207(2), 199-208. doi:10.1016/j.jsb.2019.05.008en_US
dc.identifier.issn1047-8477en_US
dc.identifier.urihttps://hdl.handle.net/10356/139321-
dc.description.abstractIn contrast to other prokaryotes, the Mycobacterial F1FO ATP synthase (α3:β3:γ:δ:ε:a:b:b’:c9) is essential for growth. The mycobacterial enzyme is also unique as a result of its 111 amino acids extended δ subunit, whose gene is fused to the peripheral stalk subunit b. Recently, the crystallographic structures of the mycobacterial α3:β3:γ:ε-domain and c subunit ring were resolved. Here, we report the first purification protocol of the intact M. smegmatis F1FO ATP synthase including the F1-domain, the entire membrane-embedded FO sector, and the stator subunits b’ and the fused b-δ. This enzyme purification enabled the determination of the first projected 2D- and 3D structure of the intact M. smegmatis F1FO ATP synthase by electron microscopy (EM) and single particle analysis. Expression and purification of the fused mycobacterial b-δ24-446 construct, excluding the membrane-embedded N-terminal amino acids, provided insight into its secondary structure. By combining these data with homology and ab-initio modeling techniques, a model of the mycobacterial peripheral stalk subunits b-δ and b’ was generated. Superposition of the 3D M. smegmatis F-ATP synthase EM-structure, the α3:β3:γ:ε and c-ring, and the derived structural models of the peripheral stalk enabled a clear assignment of all F-ATP synthase subunits, in particular with respect to the unique mycobacterial peripheral stalk subunit b’ and the elongated δ fused with subunit b. The arrangement of δ relative to the N-termini of the catalytic α3β3-headpiece and its potential as a drug target are discussed.en_US
dc.description.sponsorshipNRF (Natl Research Foundation, S’pore)en_US
dc.language.isoenen_US
dc.relationNRF–CRP18–2017–01en_US
dc.relation.ispartofJournal of structural biologyen_US
dc.rights© 2019 Elsevier Inc. All rights reserved. This paper was published in Journal of structural biology and is made available with permission of Elsevier Inc.en_US
dc.subjectScience::Biological sciences::Biochemistryen_US
dc.subjectScience::Biological sciences::Molecular biologyen_US
dc.titleStructure and subunit arrangement of Mycobacterial F1FO ATP synthase and novel features of the unique mycobacterial subunit δen_US
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.contributor.organizationNTU Institute of Structural Biologyen_US
dc.identifier.doi10.1016/j.jsb.2019.05.008-
dc.description.versionAccepted versionen_US
dc.identifier.pmid31132404-
dc.identifier.scopus2-s2.0-85066283780-
dc.identifier.issue2en_US
dc.identifier.volume207en_US
dc.identifier.spage199en_US
dc.identifier.epage208en_US
dc.subject.keywordsF-ATP Synthaseen_US
dc.subject.keywordsSubunit δen_US
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