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Title: Characterization of the Nqo5 subunit of bacterial complex I in the isolated state
Authors: Hanazono, Yuya
Takeda, Kazuki  kyouindb  KAKEN_id  orcid (unconfirmed)
Miki, Kunio  kyouindb  KAKEN_id
Author's alias: 竹田, 一旗
三木, 邦夫
Keywords: 30-Kd subunit motif
Crystal structure
NADH:ubiquinone oxidoreductase
Issue Date: Jul-2016
Publisher: FEBS Press and John Wiley & Sons Ltd.
Journal title: FEBS Open Bio
Volume: 6
Issue: 7
Start page: 687
End page: 695
Abstract: The subunits that comprise bacterial complex I (NADH:ubiquinone oxidoreductase) are also found in more complicated mitochondrial enzymes in eukaryotic organisms. Although the Nqo5 subunit is one of these conserved components and important for the formation of complex, it has been little studied. Here, we report structure analyses of isolated Nqo5 from Thermus thermophilus. Biochemical studies indicated that the C-terminal region following the 30-Kd subunit motif is disordered in the isolated state, while the remaining portion is already folded. Crystallographic studies of a trypsin-resistant fragment revealed detailed structural differences in the folded domain between the isolated and complexed states.
Rights: © 2016 The Authors. Published by FEBS Press and John Wiley & Sons Ltd.
This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
DOI(Published Version): 10.1002/2211-5463.12070
PubMed ID: 27398308
Appears in Collections:Journal Articles

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