Conformational motion of the ABC transporter MsbA induced by ATP hydrolysis.

We measured the amplitude of conformational motion in the ATP-binding cassette (ABC) transporter MsbA upon lipopolysaccharide (LPS) binding and following ATP turnover by pulse double electron-electron resonance and fluorescence homotransfer. The distance constraints from both methods reveal large-sc...

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Autores principales:	Peter P Borbat, Kavitha Surendhran, Marco Bortolus, Ping Zou, Jack H Freed, Hassane S Mchaourab
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2007
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/f040b1aa281a4fcf8179a55319ae6214
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spelling	oai:doaj.org-article:f040b1aa281a4fcf8179a55319ae62142021-11-25T05:33:07ZConformational motion of the ABC transporter MsbA induced by ATP hydrolysis.1544-91731545-788510.1371/journal.pbio.0050271https://doaj.org/article/f040b1aa281a4fcf8179a55319ae62142007-10-01T00:00:00Zhttps://doi.org/10.1371/journal.pbio.0050271https://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885We measured the amplitude of conformational motion in the ATP-binding cassette (ABC) transporter MsbA upon lipopolysaccharide (LPS) binding and following ATP turnover by pulse double electron-electron resonance and fluorescence homotransfer. The distance constraints from both methods reveal large-scale movement of opposite signs in the periplasmic and cytoplasmic part of the transporter upon ATP hydrolysis. LPS induces distinct structural changes that are inhibited by trapping of the transporter in an ATP post-hydrolysis intermediate. The formation of this intermediate involves a 33-A distance change between the two ABCs, which is consistent with a dimerization-dissociation cycle during transport that leads to their substantial separation in the absence of nucleotides. Our results suggest that ATP-powered transport entails LPS sequestering into the open cytoplasmic chamber prior to its translocation by alternating access of the chamber, made possible by 10-20-A conformational changes.Peter P BorbatKavitha SurendhranMarco BortolusPing ZouJack H FreedHassane S MchaourabPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 5, Iss 10, p e271 (2007)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Peter P Borbat Kavitha Surendhran Marco Bortolus Ping Zou Jack H Freed Hassane S Mchaourab Conformational motion of the ABC transporter MsbA induced by ATP hydrolysis.
description	We measured the amplitude of conformational motion in the ATP-binding cassette (ABC) transporter MsbA upon lipopolysaccharide (LPS) binding and following ATP turnover by pulse double electron-electron resonance and fluorescence homotransfer. The distance constraints from both methods reveal large-scale movement of opposite signs in the periplasmic and cytoplasmic part of the transporter upon ATP hydrolysis. LPS induces distinct structural changes that are inhibited by trapping of the transporter in an ATP post-hydrolysis intermediate. The formation of this intermediate involves a 33-A distance change between the two ABCs, which is consistent with a dimerization-dissociation cycle during transport that leads to their substantial separation in the absence of nucleotides. Our results suggest that ATP-powered transport entails LPS sequestering into the open cytoplasmic chamber prior to its translocation by alternating access of the chamber, made possible by 10-20-A conformational changes.
format	article
author	Peter P Borbat Kavitha Surendhran Marco Bortolus Ping Zou Jack H Freed Hassane S Mchaourab
author_facet	Peter P Borbat Kavitha Surendhran Marco Bortolus Ping Zou Jack H Freed Hassane S Mchaourab
author_sort	Peter P Borbat
title	Conformational motion of the ABC transporter MsbA induced by ATP hydrolysis.
title_short	Conformational motion of the ABC transporter MsbA induced by ATP hydrolysis.
title_full	Conformational motion of the ABC transporter MsbA induced by ATP hydrolysis.
title_fullStr	Conformational motion of the ABC transporter MsbA induced by ATP hydrolysis.
title_full_unstemmed	Conformational motion of the ABC transporter MsbA induced by ATP hydrolysis.
title_sort	conformational motion of the abc transporter msba induced by atp hydrolysis.
publisher	Public Library of Science (PLoS)
publishDate	2007
url	https://doaj.org/article/f040b1aa281a4fcf8179a55319ae6214
work_keys_str_mv	AT peterpborbat conformationalmotionoftheabctransportermsbainducedbyatphydrolysis AT kavithasurendhran conformationalmotionoftheabctransportermsbainducedbyatphydrolysis AT marcobortolus conformationalmotionoftheabctransportermsbainducedbyatphydrolysis AT pingzou conformationalmotionoftheabctransportermsbainducedbyatphydrolysis AT jackhfreed conformationalmotionoftheabctransportermsbainducedbyatphydrolysis AT hassanesmchaourab conformationalmotionoftheabctransportermsbainducedbyatphydrolysis
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Conformational motion of the ABC transporter MsbA induced by ATP hydrolysis.

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