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Comprehensive Collection and Prediction of ABC Transmembrane Protein Structures in the AI Era of Structural Biology

The number of unique transmembrane (TM) protein structures doubled in the last four years, which can be attributed to the revolution of cryo-electron microscopy. In addition, AlphaFold2 (AF2) also provided a large number of predicted structures with high quality. However, if a specific protein famil...

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Autores principales: Tordai, Hedvig, Suhajda, Erzsebet, Sillitoe, Ian, Nair, Sreenath, Varadi, Mihaly, Hegedus, Tamas
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9408558/
https://www.ncbi.nlm.nih.gov/pubmed/36012140
http://dx.doi.org/10.3390/ijms23168877
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author Tordai, Hedvig
Suhajda, Erzsebet
Sillitoe, Ian
Nair, Sreenath
Varadi, Mihaly
Hegedus, Tamas
author_facet Tordai, Hedvig
Suhajda, Erzsebet
Sillitoe, Ian
Nair, Sreenath
Varadi, Mihaly
Hegedus, Tamas
author_sort Tordai, Hedvig
collection PubMed
description The number of unique transmembrane (TM) protein structures doubled in the last four years, which can be attributed to the revolution of cryo-electron microscopy. In addition, AlphaFold2 (AF2) also provided a large number of predicted structures with high quality. However, if a specific protein family is the subject of a study, collecting the structures of the family members is highly challenging in spite of existing general and protein domain-specific databases. Here, we demonstrate this and assess the applicability and usability of automatic collection and presentation of protein structures via the ABC protein superfamily. Our pipeline identifies and classifies transmembrane ABC protein structures using the PFAM search and also aims to determine their conformational states based on special geometric measures, conftors. Since the AlphaFold database contains structure predictions only for single polypeptide chains, we performed AF2-Multimer predictions for human ABC half transporters functioning as dimers. Our AF2 predictions warn of possibly ambiguous interpretation of some biochemical data regarding interaction partners and call for further experiments and experimental structure determination. We made our predicted ABC protein structures available through a web application, and we joined the 3D-Beacons Network to reach the broader scientific community through platforms such as PDBe-KB.
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spelling pubmed-94085582022-08-26 Comprehensive Collection and Prediction of ABC Transmembrane Protein Structures in the AI Era of Structural Biology Tordai, Hedvig Suhajda, Erzsebet Sillitoe, Ian Nair, Sreenath Varadi, Mihaly Hegedus, Tamas Int J Mol Sci Article The number of unique transmembrane (TM) protein structures doubled in the last four years, which can be attributed to the revolution of cryo-electron microscopy. In addition, AlphaFold2 (AF2) also provided a large number of predicted structures with high quality. However, if a specific protein family is the subject of a study, collecting the structures of the family members is highly challenging in spite of existing general and protein domain-specific databases. Here, we demonstrate this and assess the applicability and usability of automatic collection and presentation of protein structures via the ABC protein superfamily. Our pipeline identifies and classifies transmembrane ABC protein structures using the PFAM search and also aims to determine their conformational states based on special geometric measures, conftors. Since the AlphaFold database contains structure predictions only for single polypeptide chains, we performed AF2-Multimer predictions for human ABC half transporters functioning as dimers. Our AF2 predictions warn of possibly ambiguous interpretation of some biochemical data regarding interaction partners and call for further experiments and experimental structure determination. We made our predicted ABC protein structures available through a web application, and we joined the 3D-Beacons Network to reach the broader scientific community through platforms such as PDBe-KB. MDPI 2022-08-09 /pmc/articles/PMC9408558/ /pubmed/36012140 http://dx.doi.org/10.3390/ijms23168877 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Tordai, Hedvig
Suhajda, Erzsebet
Sillitoe, Ian
Nair, Sreenath
Varadi, Mihaly
Hegedus, Tamas
Comprehensive Collection and Prediction of ABC Transmembrane Protein Structures in the AI Era of Structural Biology
title Comprehensive Collection and Prediction of ABC Transmembrane Protein Structures in the AI Era of Structural Biology
title_full Comprehensive Collection and Prediction of ABC Transmembrane Protein Structures in the AI Era of Structural Biology
title_fullStr Comprehensive Collection and Prediction of ABC Transmembrane Protein Structures in the AI Era of Structural Biology
title_full_unstemmed Comprehensive Collection and Prediction of ABC Transmembrane Protein Structures in the AI Era of Structural Biology
title_short Comprehensive Collection and Prediction of ABC Transmembrane Protein Structures in the AI Era of Structural Biology
title_sort comprehensive collection and prediction of abc transmembrane protein structures in the ai era of structural biology
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9408558/
https://www.ncbi.nlm.nih.gov/pubmed/36012140
http://dx.doi.org/10.3390/ijms23168877
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