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Plant Lessons: Exploring ABCB Functionality Through Structural Modeling

In contrast to mammalian ABCB1 proteins, narrow substrate specificity has been extensively documented for plant orthologs shown to catalyze the transport of the plant hormone, auxin. Using the crystal structures of the multidrug exporters Sav1866 and MmABCB1 as templates, we have developed structura...

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Autores principales: Bailly, Aurélien, Yang, Haibing, Martinoia, Enrico, Geisler, Markus, Murphy, Angus S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Research Foundation 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3355715/
https://www.ncbi.nlm.nih.gov/pubmed/22639627
http://dx.doi.org/10.3389/fpls.2011.00108
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author Bailly, Aurélien
Yang, Haibing
Martinoia, Enrico
Geisler, Markus
Murphy, Angus S.
author_facet Bailly, Aurélien
Yang, Haibing
Martinoia, Enrico
Geisler, Markus
Murphy, Angus S.
author_sort Bailly, Aurélien
collection PubMed
description In contrast to mammalian ABCB1 proteins, narrow substrate specificity has been extensively documented for plant orthologs shown to catalyze the transport of the plant hormone, auxin. Using the crystal structures of the multidrug exporters Sav1866 and MmABCB1 as templates, we have developed structural models of plant ABCB proteins with a common architecture. Comparisons of these structures identified kingdom-specific candidate substrate-binding regions within the translocation chamber formed by the transmembrane domains of ABCBs from the model plant Arabidopsis. These results suggest an early evolutionary divergence of plant and mammalian ABCBs. Validation of these models becomes a priority for efforts to elucidate ABCB function and manipulate this class of transporters to enhance plant productivity and quality.
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spelling pubmed-33557152012-05-25 Plant Lessons: Exploring ABCB Functionality Through Structural Modeling Bailly, Aurélien Yang, Haibing Martinoia, Enrico Geisler, Markus Murphy, Angus S. Front Plant Sci Plant Science In contrast to mammalian ABCB1 proteins, narrow substrate specificity has been extensively documented for plant orthologs shown to catalyze the transport of the plant hormone, auxin. Using the crystal structures of the multidrug exporters Sav1866 and MmABCB1 as templates, we have developed structural models of plant ABCB proteins with a common architecture. Comparisons of these structures identified kingdom-specific candidate substrate-binding regions within the translocation chamber formed by the transmembrane domains of ABCBs from the model plant Arabidopsis. These results suggest an early evolutionary divergence of plant and mammalian ABCBs. Validation of these models becomes a priority for efforts to elucidate ABCB function and manipulate this class of transporters to enhance plant productivity and quality. Frontiers Research Foundation 2012-01-05 /pmc/articles/PMC3355715/ /pubmed/22639627 http://dx.doi.org/10.3389/fpls.2011.00108 Text en Copyright © 2012 Bailly, Yang, Martinoia, Geisler and Murphy. http://www.frontiersin.org/licenseagreement This is an open-access article distributed under the terms of the Creative Commons Attribution Non Commercial License, which permits non-commercial use, distribution, and reproduction in other forums, provided the original authors and source are credited.
spellingShingle Plant Science
Bailly, Aurélien
Yang, Haibing
Martinoia, Enrico
Geisler, Markus
Murphy, Angus S.
Plant Lessons: Exploring ABCB Functionality Through Structural Modeling
title Plant Lessons: Exploring ABCB Functionality Through Structural Modeling
title_full Plant Lessons: Exploring ABCB Functionality Through Structural Modeling
title_fullStr Plant Lessons: Exploring ABCB Functionality Through Structural Modeling
title_full_unstemmed Plant Lessons: Exploring ABCB Functionality Through Structural Modeling
title_short Plant Lessons: Exploring ABCB Functionality Through Structural Modeling
title_sort plant lessons: exploring abcb functionality through structural modeling
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3355715/
https://www.ncbi.nlm.nih.gov/pubmed/22639627
http://dx.doi.org/10.3389/fpls.2011.00108
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