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Smoothing membrane protein structure determination by initial upstream stage improvements
Membrane proteins (MP) constitute 20–30% of all proteins encoded by the genome of various organisms and perform a wide range of essential biological functions. However, despite they represent the largest class of protein drug targets, a relatively small number high-resolution 3D structures have been...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7079970/ https://www.ncbi.nlm.nih.gov/pubmed/31127356 http://dx.doi.org/10.1007/s00253-019-09873-1 |
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author | Pedro, Augusto Quaresma Queiroz, João António Passarinha, Luís António |
author_facet | Pedro, Augusto Quaresma Queiroz, João António Passarinha, Luís António |
author_sort | Pedro, Augusto Quaresma |
collection | PubMed |
description | Membrane proteins (MP) constitute 20–30% of all proteins encoded by the genome of various organisms and perform a wide range of essential biological functions. However, despite they represent the largest class of protein drug targets, a relatively small number high-resolution 3D structures have been obtained yet. Membrane protein biogenesis is more complex than that of the soluble proteins and its recombinant biosynthesis has been a major drawback, thus delaying their further structural characterization. Indeed, the major limitation in structure determination of MP is the low yield achieved in recombinant expression, usually coupled to low functionality, pinpointing the optimization target in recombinant MP research. Recently, the growing attention that have been dedicated to the upstream stage of MP bioprocesses allowed great advances, permitting the evolution of the number of MP solved structures. In this review, we analyse and discuss effective solutions and technical advances at the level of the upstream stage using prokaryotic and eukaryotic organisms foreseeing an increase in expression yields of correctly folded MP and that may facilitate the determination of their three-dimensional structure. A section on techniques used to protein quality control and further structure determination of MP is also included. Lastly, a critical assessment of major factors contributing for a good decision-making process related to the upstream stage of MP is presented. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s00253-019-09873-1) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-7079970 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-70799702020-03-23 Smoothing membrane protein structure determination by initial upstream stage improvements Pedro, Augusto Quaresma Queiroz, João António Passarinha, Luís António Appl Microbiol Biotechnol Mini-Review Membrane proteins (MP) constitute 20–30% of all proteins encoded by the genome of various organisms and perform a wide range of essential biological functions. However, despite they represent the largest class of protein drug targets, a relatively small number high-resolution 3D structures have been obtained yet. Membrane protein biogenesis is more complex than that of the soluble proteins and its recombinant biosynthesis has been a major drawback, thus delaying their further structural characterization. Indeed, the major limitation in structure determination of MP is the low yield achieved in recombinant expression, usually coupled to low functionality, pinpointing the optimization target in recombinant MP research. Recently, the growing attention that have been dedicated to the upstream stage of MP bioprocesses allowed great advances, permitting the evolution of the number of MP solved structures. In this review, we analyse and discuss effective solutions and technical advances at the level of the upstream stage using prokaryotic and eukaryotic organisms foreseeing an increase in expression yields of correctly folded MP and that may facilitate the determination of their three-dimensional structure. A section on techniques used to protein quality control and further structure determination of MP is also included. Lastly, a critical assessment of major factors contributing for a good decision-making process related to the upstream stage of MP is presented. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s00253-019-09873-1) contains supplementary material, which is available to authorized users. Springer Berlin Heidelberg 2019-05-24 2019 /pmc/articles/PMC7079970/ /pubmed/31127356 http://dx.doi.org/10.1007/s00253-019-09873-1 Text en © Springer-Verlag GmbH Germany, part of Springer Nature 2019 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic. |
spellingShingle | Mini-Review Pedro, Augusto Quaresma Queiroz, João António Passarinha, Luís António Smoothing membrane protein structure determination by initial upstream stage improvements |
title | Smoothing membrane protein structure determination by initial upstream stage improvements |
title_full | Smoothing membrane protein structure determination by initial upstream stage improvements |
title_fullStr | Smoothing membrane protein structure determination by initial upstream stage improvements |
title_full_unstemmed | Smoothing membrane protein structure determination by initial upstream stage improvements |
title_short | Smoothing membrane protein structure determination by initial upstream stage improvements |
title_sort | smoothing membrane protein structure determination by initial upstream stage improvements |
topic | Mini-Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7079970/ https://www.ncbi.nlm.nih.gov/pubmed/31127356 http://dx.doi.org/10.1007/s00253-019-09873-1 |
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