High-resolution NMR reveals secondary structure and folding of amino acid transporter from outer chloroplast membrane.

Solving high-resolution structures for membrane proteins continues to be a daunting challenge in the structural biology community. In this study we report our high-resolution NMR results for a transmembrane protein, outer envelope protein of molar mass 16 kDa (OEP16), an amino acid transporter from...

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Autores principales:	James D Zook, Trivikram R Molugu, Neil E Jacobsen, Guangxin Lin, Jürgen Soll, Brian R Cherry, Michael F Brown, Petra Fromme
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/50457bd529314342ae0acd763540684c
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spelling	oai:doaj.org-article:50457bd529314342ae0acd763540684c2021-11-18T08:49:07ZHigh-resolution NMR reveals secondary structure and folding of amino acid transporter from outer chloroplast membrane.1932-620310.1371/journal.pone.0078116https://doaj.org/article/50457bd529314342ae0acd763540684c2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24205117/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Solving high-resolution structures for membrane proteins continues to be a daunting challenge in the structural biology community. In this study we report our high-resolution NMR results for a transmembrane protein, outer envelope protein of molar mass 16 kDa (OEP16), an amino acid transporter from the outer membrane of chloroplasts. Three-dimensional, high-resolution NMR experiments on the (13)C, (15)N, (2)H-triply-labeled protein were used to assign protein backbone resonances and to obtain secondary structure information. The results yield over 95% assignment of N, HN, CO, Cα, and Cβ chemical shifts, which is essential for obtaining a high resolution structure from NMR data. Chemical shift analysis from the assignment data reveals experimental evidence for the first time on the location of the secondary structure elements on a per residue basis. In addition T 1Z and T2 relaxation experiments were performed in order to better understand the protein dynamics. Arginine titration experiments yield an insight into the amino acid residues responsible for protein transporter function. The results provide the necessary basis for high-resolution structural determination of this important plant membrane protein.James D ZookTrivikram R MoluguNeil E JacobsenGuangxin LinJürgen SollBrian R CherryMichael F BrownPetra FrommePublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 10, p e78116 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q James D Zook Trivikram R Molugu Neil E Jacobsen Guangxin Lin Jürgen Soll Brian R Cherry Michael F Brown Petra Fromme High-resolution NMR reveals secondary structure and folding of amino acid transporter from outer chloroplast membrane.
description	Solving high-resolution structures for membrane proteins continues to be a daunting challenge in the structural biology community. In this study we report our high-resolution NMR results for a transmembrane protein, outer envelope protein of molar mass 16 kDa (OEP16), an amino acid transporter from the outer membrane of chloroplasts. Three-dimensional, high-resolution NMR experiments on the (13)C, (15)N, (2)H-triply-labeled protein were used to assign protein backbone resonances and to obtain secondary structure information. The results yield over 95% assignment of N, HN, CO, Cα, and Cβ chemical shifts, which is essential for obtaining a high resolution structure from NMR data. Chemical shift analysis from the assignment data reveals experimental evidence for the first time on the location of the secondary structure elements on a per residue basis. In addition T 1Z and T2 relaxation experiments were performed in order to better understand the protein dynamics. Arginine titration experiments yield an insight into the amino acid residues responsible for protein transporter function. The results provide the necessary basis for high-resolution structural determination of this important plant membrane protein.
format	article
author	James D Zook Trivikram R Molugu Neil E Jacobsen Guangxin Lin Jürgen Soll Brian R Cherry Michael F Brown Petra Fromme
author_facet	James D Zook Trivikram R Molugu Neil E Jacobsen Guangxin Lin Jürgen Soll Brian R Cherry Michael F Brown Petra Fromme
author_sort	James D Zook
title	High-resolution NMR reveals secondary structure and folding of amino acid transporter from outer chloroplast membrane.
title_short	High-resolution NMR reveals secondary structure and folding of amino acid transporter from outer chloroplast membrane.
title_full	High-resolution NMR reveals secondary structure and folding of amino acid transporter from outer chloroplast membrane.
title_fullStr	High-resolution NMR reveals secondary structure and folding of amino acid transporter from outer chloroplast membrane.
title_full_unstemmed	High-resolution NMR reveals secondary structure and folding of amino acid transporter from outer chloroplast membrane.
title_sort	high-resolution nmr reveals secondary structure and folding of amino acid transporter from outer chloroplast membrane.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/50457bd529314342ae0acd763540684c
work_keys_str_mv	AT jamesdzook highresolutionnmrrevealssecondarystructureandfoldingofaminoacidtransporterfromouterchloroplastmembrane AT trivikramrmolugu highresolutionnmrrevealssecondarystructureandfoldingofaminoacidtransporterfromouterchloroplastmembrane AT neilejacobsen highresolutionnmrrevealssecondarystructureandfoldingofaminoacidtransporterfromouterchloroplastmembrane AT guangxinlin highresolutionnmrrevealssecondarystructureandfoldingofaminoacidtransporterfromouterchloroplastmembrane AT jurgensoll highresolutionnmrrevealssecondarystructureandfoldingofaminoacidtransporterfromouterchloroplastmembrane AT brianrcherry highresolutionnmrrevealssecondarystructureandfoldingofaminoacidtransporterfromouterchloroplastmembrane AT michaelfbrown highresolutionnmrrevealssecondarystructureandfoldingofaminoacidtransporterfromouterchloroplastmembrane AT petrafromme highresolutionnmrrevealssecondarystructureandfoldingofaminoacidtransporterfromouterchloroplastmembrane
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High-resolution NMR reveals secondary structure and folding of amino acid transporter from outer chloroplast membrane.

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