Characterization of the Nqo5 subunit of bacterial complex I in the isolated state

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. Her...

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Main Authors:	Hanazono, Yuya, Takeda, Kazuki, Miki, Kunio
Format:	Online
Language:	English
Published:	John Wiley and Sons Inc. 2016
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4932448/

id	pubmed-4932448
recordtype	oai_dc
spelling	pubmed-49324482016-07-08 Characterization of the Nqo5 subunit of bacterial complex I in the isolated state Hanazono, Yuya Takeda, Kazuki Miki, Kunio Research Articles 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. John Wiley and Sons Inc. 2016-06-08 /pmc/articles/PMC4932448/ /pubmed/27398308 http://dx.doi.org/10.1002/2211-5463.12070 Text en © 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 (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Hanazono, Yuya Takeda, Kazuki Miki, Kunio
spellingShingle	Hanazono, Yuya Takeda, Kazuki Miki, Kunio Characterization of the Nqo5 subunit of bacterial complex I in the isolated state
author_facet	Hanazono, Yuya Takeda, Kazuki Miki, Kunio
author_sort	Hanazono, Yuya
title	Characterization of the Nqo5 subunit of bacterial complex I in the isolated state
title_short	Characterization of the Nqo5 subunit of bacterial complex I in the isolated state
title_full	Characterization of the Nqo5 subunit of bacterial complex I in the isolated state
title_fullStr	Characterization of the Nqo5 subunit of bacterial complex I in the isolated state
title_full_unstemmed	Characterization of the Nqo5 subunit of bacterial complex I in the isolated state
title_sort	characterization of the nqo5 subunit of bacterial complex i in the isolated state
description	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.
publisher	John Wiley and Sons Inc.
publishDate	2016
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4932448/
_version_	1613604120729485312

Characterization of the Nqo5 subunit of bacterial complex I in the isolated state

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