Structural insights into polyamine spermidine uptake by the ABC transporter PotD-PotABC

Polyamines, characterized by their polycationic nature, are ubiquitously present in all organisms and play numerous cellular functions. Among polyamines, spermidine stands out as the predominant type in both prokaryotic and eukaryotic cells. The PotD-PotABC protein complex in Escherichia coli, belon...

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Main Authors: Qiao, Zhu, Do, Phong Hoa, Yeo, Joshua Yi, Ero, Rya, Li, Zhuowen, Zhan, Liying, Basak, Sandip, Gao, Yong-Gui
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2024
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Online Access:https://hdl.handle.net/10356/180453
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-1804532024-10-14T15:31:58Z Structural insights into polyamine spermidine uptake by the ABC transporter PotD-PotABC Qiao, Zhu Do, Phong Hoa Yeo, Joshua Yi Ero, Rya Li, Zhuowen Zhan, Liying Basak, Sandip Gao, Yong-Gui School of Biological Sciences NTU Institute of Structural Biology Medicine, Health and Life Sciences ABC transporter Cellular function Polyamines, characterized by their polycationic nature, are ubiquitously present in all organisms and play numerous cellular functions. Among polyamines, spermidine stands out as the predominant type in both prokaryotic and eukaryotic cells. The PotD-PotABC protein complex in Escherichia coli, belonging to the adenosine triphosphate-binding cassette transporter family, is a spermidine-preferential uptake system. Here, we report structural details of the polyamine uptake system PotD-PotABC in various states. Our analyses reveal distinct "inward-facing" and "outward-facing" conformations of the PotD-PotABC transporter, as well as conformational changes in the "gating" residues (F222, Y223, D226, and K241 in PotB; Y219 and K223 in PotC) controlling spermidine uptake. Therefore, our structural analysis provides insights into how the PotD-PotABC importer recognizes the substrate-binding protein PotD and elucidates molecular insights into the spermidine uptake mechanism of bacteria. Ministry of Education (MOE) Published version This work was supported by a Tier II grant MOE-T2EP30122-0019 from the Ministry of education (MOE) of Singapore (Y.-G.G.). 2024-10-08T01:39:32Z 2024-10-08T01:39:32Z 2024 Journal Article Qiao, Z., Do, P. H., Yeo, J. Y., Ero, R., Li, Z., Zhan, L., Basak, S. & Gao, Y. (2024). Structural insights into polyamine spermidine uptake by the ABC transporter PotD-PotABC. Science Advances, 10(38), eado8107-. https://dx.doi.org/10.1126/sciadv.ado8107 2375-2548 https://hdl.handle.net/10356/180453 10.1126/sciadv.ado8107 39303029 2-s2.0-85204512430 38 10 eado8107 en MOE-T2EP30122-0019 Science Advances © 2024 the Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a creative commons Attribution license 4.0(CC BY). application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic Medicine, Health and Life Sciences
ABC transporter
Cellular function
spellingShingle Medicine, Health and Life Sciences
ABC transporter
Cellular function
Qiao, Zhu
Do, Phong Hoa
Yeo, Joshua Yi
Ero, Rya
Li, Zhuowen
Zhan, Liying
Basak, Sandip
Gao, Yong-Gui
Structural insights into polyamine spermidine uptake by the ABC transporter PotD-PotABC
description Polyamines, characterized by their polycationic nature, are ubiquitously present in all organisms and play numerous cellular functions. Among polyamines, spermidine stands out as the predominant type in both prokaryotic and eukaryotic cells. The PotD-PotABC protein complex in Escherichia coli, belonging to the adenosine triphosphate-binding cassette transporter family, is a spermidine-preferential uptake system. Here, we report structural details of the polyamine uptake system PotD-PotABC in various states. Our analyses reveal distinct "inward-facing" and "outward-facing" conformations of the PotD-PotABC transporter, as well as conformational changes in the "gating" residues (F222, Y223, D226, and K241 in PotB; Y219 and K223 in PotC) controlling spermidine uptake. Therefore, our structural analysis provides insights into how the PotD-PotABC importer recognizes the substrate-binding protein PotD and elucidates molecular insights into the spermidine uptake mechanism of bacteria.
author2 School of Biological Sciences
author_facet School of Biological Sciences
Qiao, Zhu
Do, Phong Hoa
Yeo, Joshua Yi
Ero, Rya
Li, Zhuowen
Zhan, Liying
Basak, Sandip
Gao, Yong-Gui
format Article
author Qiao, Zhu
Do, Phong Hoa
Yeo, Joshua Yi
Ero, Rya
Li, Zhuowen
Zhan, Liying
Basak, Sandip
Gao, Yong-Gui
author_sort Qiao, Zhu
title Structural insights into polyamine spermidine uptake by the ABC transporter PotD-PotABC
title_short Structural insights into polyamine spermidine uptake by the ABC transporter PotD-PotABC
title_full Structural insights into polyamine spermidine uptake by the ABC transporter PotD-PotABC
title_fullStr Structural insights into polyamine spermidine uptake by the ABC transporter PotD-PotABC
title_full_unstemmed Structural insights into polyamine spermidine uptake by the ABC transporter PotD-PotABC
title_sort structural insights into polyamine spermidine uptake by the abc transporter potd-potabc
publishDate 2024
url https://hdl.handle.net/10356/180453
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