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DC Field | Value | Language |
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dc.contributor.author | Kamariah, Neelagandan | en_US |
dc.contributor.author | Huber, Roland G. | en_US |
dc.contributor.author | Nartey, Wilson | en_US |
dc.contributor.author | Bhushan, Shashi | en_US |
dc.contributor.author | Bond, Peter J. | en_US |
dc.contributor.author | Grüber, Gerhard | en_US |
dc.date.accessioned | 2020-05-19T01:17:30Z | - |
dc.date.available | 2020-05-19T01:17:30Z | - |
dc.date.issued | 2019 | - |
dc.identifier.citation | Kamariah, 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.2019.05.008 | en_US |
dc.identifier.issn | 1047-8477 | en_US |
dc.identifier.uri | https://hdl.handle.net/10356/139321 | - |
dc.description.abstract | In 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.sponsorship | NRF (Natl Research Foundation, S’pore) | en_US |
dc.language.iso | en | en_US |
dc.relation | NRF–CRP18–2017–01 | en_US |
dc.relation.ispartof | Journal of structural biology | en_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.subject | Science::Biological sciences::Biochemistry | en_US |
dc.subject | Science::Biological sciences::Molecular biology | en_US |
dc.title | Structure and subunit arrangement of Mycobacterial F1FO ATP synthase and novel features of the unique mycobacterial subunit δ | en_US |
dc.type | Journal Article | en |
dc.contributor.school | School of Biological Sciences | en_US |
dc.contributor.organization | NTU Institute of Structural Biology | en_US |
dc.identifier.doi | 10.1016/j.jsb.2019.05.008 | - |
dc.description.version | Accepted version | en_US |
dc.identifier.pmid | 31132404 | - |
dc.identifier.scopus | 2-s2.0-85066283780 | - |
dc.identifier.issue | 2 | en_US |
dc.identifier.volume | 207 | en_US |
dc.identifier.spage | 199 | en_US |
dc.identifier.epage | 208 | en_US |
dc.subject.keywords | F-ATP Synthase | en_US |
dc.subject.keywords | Subunit δ | en_US |
item.fulltext | With Fulltext | - |
item.grantfulltext | open | - |
Appears in Collections: | SBS Journal Articles |
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File | Description | Size | Format | |
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Kamariah_etal_JSB.pdf | 1.32 MB | Adobe PDF | View/Open |
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