Small-angle neutron scattering reveals the assembly mode and oligomeric architecture of TET, a large, dodecameric aminopeptidase

The present work illustrates that small-angle neutron scattering, deuteration and contrast variation, combined with in vitro particle reconstruction, constitutes a very efficient approach to determine subunit architectures in large, symmetric protein complexes. In the case of the 468 kDa heterododec...

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Main Authors:	Appolaire, Alexandre, Girard, Eric, Colombo, Matteo, Durá, M. Asunción, Moulin, Martine, Härtlein, Michael, Franzetti, Bruno, Gabel, Frank
Format:	Online
Language:	English
Published:	International Union of Crystallography 2014
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4220976/

id	pubmed-4220976
recordtype	oai_dc
spelling	pubmed-42209762014-11-13 Small-angle neutron scattering reveals the assembly mode and oligomeric architecture of TET, a large, dodecameric aminopeptidase Appolaire, Alexandre Girard, Eric Colombo, Matteo Durá, M. Asunción Moulin, Martine Härtlein, Michael Franzetti, Bruno Gabel, Frank Research Papers The present work illustrates that small-angle neutron scattering, deuteration and contrast variation, combined with in vitro particle reconstruction, constitutes a very efficient approach to determine subunit architectures in large, symmetric protein complexes. In the case of the 468 kDa heterododecameric TET peptidase machine, it was demonstrated that the assembly of the 12 subunits is a highly controlled process and represents a way to optimize the catalytic efficiency of the enzyme. International Union of Crystallography 2014-10-23 /pmc/articles/PMC4220976/ /pubmed/25372688 http://dx.doi.org/10.1107/S1399004714018446 Text en © Appolaire et al. 2014 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are 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	Appolaire, Alexandre Girard, Eric Colombo, Matteo Durá, M. Asunción Moulin, Martine Härtlein, Michael Franzetti, Bruno Gabel, Frank
spellingShingle	Appolaire, Alexandre Girard, Eric Colombo, Matteo Durá, M. Asunción Moulin, Martine Härtlein, Michael Franzetti, Bruno Gabel, Frank Small-angle neutron scattering reveals the assembly mode and oligomeric architecture of TET, a large, dodecameric aminopeptidase
author_facet	Appolaire, Alexandre Girard, Eric Colombo, Matteo Durá, M. Asunción Moulin, Martine Härtlein, Michael Franzetti, Bruno Gabel, Frank
author_sort	Appolaire, Alexandre
title	Small-angle neutron scattering reveals the assembly mode and oligomeric architecture of TET, a large, dodecameric aminopeptidase
title_short	Small-angle neutron scattering reveals the assembly mode and oligomeric architecture of TET, a large, dodecameric aminopeptidase
title_full	Small-angle neutron scattering reveals the assembly mode and oligomeric architecture of TET, a large, dodecameric aminopeptidase
title_fullStr	Small-angle neutron scattering reveals the assembly mode and oligomeric architecture of TET, a large, dodecameric aminopeptidase
title_full_unstemmed	Small-angle neutron scattering reveals the assembly mode and oligomeric architecture of TET, a large, dodecameric aminopeptidase
title_sort	small-angle neutron scattering reveals the assembly mode and oligomeric architecture of tet, a large, dodecameric aminopeptidase
description	The present work illustrates that small-angle neutron scattering, deuteration and contrast variation, combined with in vitro particle reconstruction, constitutes a very efficient approach to determine subunit architectures in large, symmetric protein complexes. In the case of the 468 kDa heterododecameric TET peptidase machine, it was demonstrated that the assembly of the 12 subunits is a highly controlled process and represents a way to optimize the catalytic efficiency of the enzyme.
publisher	International Union of Crystallography
publishDate	2014
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4220976/
_version_	1613152540230156288

Small-angle neutron scattering reveals the assembly mode and oligomeric architecture of TET, a large, dodecameric aminopeptidase

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