Structural and functional diversity calls for a new classification of ABC transporters

Christoph Thomas; Stephen G Aller; Konstantinos Beis; Elisabeth P Carpenter; Geoffrey Chang; Lei Chen; Elie Dassa; Michel Dean; Franck Duong Van Hoa; Damian Ekiert; Robert Ford; Rachelle Gaudet; Xin Gong; I Barry Holland; Yihua Huang; Daniel K Kahne; Hiroaki Kato; Vassilis Koronakis; Christopher M Koth; Youngsook Lee; Oded Lewinson; Roland Lill; Enrico Martinoia; Satoshi Murakami; Heather W Pinket; Bert Poolman; Daniel Rosenbaum; Balazs Sarkadi; Lutz Schmitt; Erwin Schneider; Yigong Shi; Show-Ling Shyng; Dirk J Slotboom; Emad Tajkhorshid; D Peter Tieleman; Kazumitsu Ueda; András Váradi; Po-Chao Wen; Nieng Yan; Peng Zhang; Hongjin Zheng; Jochen Zimmer; Robert Tampé

doi:10.1002/1873-3468.13935

Structural and functional diversity calls for a new classification of ABC transporters

Christoph Thomas^*, Stephen G Aller, Konstantinos Beis, Elisabeth P Carpenter, Geoffrey Chang, Lei Chen, Elie Dassa, Michel Dean, Franck Duong Van Hoa, Damian Ekiert, Robert Ford, Rachelle Gaudet, Xin Gong, I Barry Holland, Yihua Huang, Daniel K Kahne, Hiroaki Kato, Vassilis Koronakis, Christopher M Koth, Youngsook LeeOded Lewinson, Roland Lill, Enrico Martinoia, Satoshi Murakami, Heather W Pinket, Bert Poolman, Daniel Rosenbaum, Balazs Sarkadi, Lutz Schmitt, Erwin Schneider, Yigong Shi, Show-Ling Shyng, Dirk J Slotboom, Emad Tajkhorshid, D Peter Tieleman, Kazumitsu Ueda, András Váradi, Po-Chao Wen, Nieng Yan, Peng Zhang, Hongjin Zheng, Jochen Zimmer, Robert Tampé^*

^*Corresponding author voor dit werk

Enzymologie

Onderzoeksoutput › Academic › peer review

196 Citaten (Scopus)

155 Downloads (Pure)

Samenvatting

Members of the ATP-binding cassette (ABC) transporter superfamily translocate a broad spectrum of chemically diverse substrates. While their eponymous ATP-binding cassette in the nucleotide-binding domains (NBDs) is highly conserved, their transmembrane domains (TMDs) forming the translocation pathway exhibit distinct folds and topologies, suggesting that during evolution the ancient motor domains were combined with different transmembrane mechanical systems to orchestrate a variety of cellular processes. In recent years, it has become increasingly evident that the distinct TMD folds are best suited to categorize the multitude of ABC transporters. We therefore propose a new ABC transporter classification that is based on structural homology in the TMDs.

Originele taal-2	English
Artikelnummer	1873-3468.13935
Pagina's (van-tot)	3767-3775
Aantal pagina's	9
Tijdschrift	FEBS Letters
Volume	594
Nummer van het tijdschrift	23
Vroegere onlinedatum	26-sep.-2020
DOI's	https://doi.org/10.1002/1873-3468.13935
Status	Published - dec.-2020

Toegang tot document

10.1002/1873-3468.13935Licentie: CC BY

Structural and functional diversity calls for a new classification of ABC transportersFinal publisher's version, 1,05 MBLicentie: CC BY

Handle.net

Permanente koppeling

Citeer dit

Thomas, C., Aller, S. G., Beis, K., Carpenter, E. P., Chang, G., Chen, L., Dassa, E., Dean, M., Duong Van Hoa, F., Ekiert, D., Ford, R., Gaudet, R., Gong, X., Holland, I. B., Huang, Y., Kahne, D. K., Kato, H., Koronakis, V., Koth, C. M., ... Tampé, R. (2020). Structural and functional diversity calls for a new classification of ABC transporters. FEBS Letters, 594(23), 3767-3775. Artikel 1873-3468.13935. https://doi.org/10.1002/1873-3468.13935

@article{a90d1516f7d442b997e51da562f95d50,

title = "Structural and functional diversity calls for a new classification of ABC transporters",

abstract = "Members of the ATP-binding cassette (ABC) transporter superfamily translocate a broad spectrum of chemically diverse substrates. While their eponymous ATP-binding cassette in the nucleotide-binding domains (NBDs) is highly conserved, their transmembrane domains (TMDs) forming the translocation pathway exhibit distinct folds and topologies, suggesting that during evolution the ancient motor domains were combined with different transmembrane mechanical systems to orchestrate a variety of cellular processes. In recent years, it has become increasingly evident that the distinct TMD folds are best suited to categorize the multitude of ABC transporters. We therefore propose a new ABC transporter classification that is based on structural homology in the TMDs.",

keywords = "ABC transporters, ATPases, X-ray crystallography, cryo-EM, membrane proteins, molecular machines, phylogeny, primary active transporters, sequence alignment, structural biology",

author = "Christoph Thomas and Aller, {Stephen G} and Konstantinos Beis and Carpenter, {Elisabeth P} and Geoffrey Chang and Lei Chen and Elie Dassa and Michel Dean and {Duong Van Hoa}, Franck and Damian Ekiert and Robert Ford and Rachelle Gaudet and Xin Gong and Holland, {I Barry} and Yihua Huang and Kahne, {Daniel K} and Hiroaki Kato and Vassilis Koronakis and Koth, {Christopher M} and Youngsook Lee and Oded Lewinson and Roland Lill and Enrico Martinoia and Satoshi Murakami and Pinket, {Heather W} and Bert Poolman and Daniel Rosenbaum and Balazs Sarkadi and Lutz Schmitt and Erwin Schneider and Yigong Shi and Show-Ling Shyng and Slotboom, {Dirk J} and Emad Tajkhorshid and Tieleman, {D Peter} and Kazumitsu Ueda and Andr{\'a}s V{\'a}radi and Po-Chao Wen and Nieng Yan and Peng Zhang and Hongjin Zheng and Jochen Zimmer and Robert Tamp{\'e}",

year = "2020",

month = dec,

doi = "10.1002/1873-3468.13935",

language = "English",

volume = "594",

pages = "3767--3775",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Wiley",

number = "23",

}

Thomas, C, Aller, SG, Beis, K, Carpenter, EP, Chang, G, Chen, L, Dassa, E, Dean, M, Duong Van Hoa, F, Ekiert, D, Ford, R, Gaudet, R, Gong, X, Holland, IB, Huang, Y, Kahne, DK, Kato, H, Koronakis, V, Koth, CM, Lee, Y, Lewinson, O, Lill, R, Martinoia, E, Murakami, S, Pinket, HW, Poolman, B, Rosenbaum, D, Sarkadi, B, Schmitt, L, Schneider, E, Shi, Y, Shyng, S-L, Slotboom, DJ, Tajkhorshid, E, Tieleman, DP, Ueda, K, Váradi, A, Wen, P-C, Yan, N, Zhang, P, Zheng, H, Zimmer, J & Tampé, R 2020, 'Structural and functional diversity calls for a new classification of ABC transporters', FEBS Letters, vol. 594, nr. 23, 1873-3468.13935, blz. 3767-3775. https://doi.org/10.1002/1873-3468.13935

TY - JOUR

T1 - Structural and functional diversity calls for a new classification of ABC transporters

AU - Thomas, Christoph

AU - Aller, Stephen G

AU - Beis, Konstantinos

AU - Carpenter, Elisabeth P

AU - Chang, Geoffrey

AU - Chen, Lei

AU - Dassa, Elie

AU - Dean, Michel

AU - Duong Van Hoa, Franck

AU - Ekiert, Damian

AU - Ford, Robert

AU - Gaudet, Rachelle

AU - Gong, Xin

AU - Holland, I Barry

AU - Huang, Yihua

AU - Kahne, Daniel K

AU - Kato, Hiroaki

AU - Koronakis, Vassilis

AU - Koth, Christopher M

AU - Lee, Youngsook

AU - Lewinson, Oded

AU - Lill, Roland

AU - Martinoia, Enrico

AU - Murakami, Satoshi

AU - Pinket, Heather W

AU - Poolman, Bert

AU - Rosenbaum, Daniel

AU - Sarkadi, Balazs

AU - Schmitt, Lutz

AU - Schneider, Erwin

AU - Shi, Yigong

AU - Shyng, Show-Ling

AU - Slotboom, Dirk J

AU - Tajkhorshid, Emad

AU - Tieleman, D Peter

AU - Ueda, Kazumitsu

AU - Váradi, András

AU - Wen, Po-Chao

AU - Yan, Nieng

AU - Zhang, Peng

AU - Zheng, Hongjin

AU - Zimmer, Jochen

AU - Tampé, Robert

PY - 2020/12

Y1 - 2020/12

N2 - Members of the ATP-binding cassette (ABC) transporter superfamily translocate a broad spectrum of chemically diverse substrates. While their eponymous ATP-binding cassette in the nucleotide-binding domains (NBDs) is highly conserved, their transmembrane domains (TMDs) forming the translocation pathway exhibit distinct folds and topologies, suggesting that during evolution the ancient motor domains were combined with different transmembrane mechanical systems to orchestrate a variety of cellular processes. In recent years, it has become increasingly evident that the distinct TMD folds are best suited to categorize the multitude of ABC transporters. We therefore propose a new ABC transporter classification that is based on structural homology in the TMDs.

AB - Members of the ATP-binding cassette (ABC) transporter superfamily translocate a broad spectrum of chemically diverse substrates. While their eponymous ATP-binding cassette in the nucleotide-binding domains (NBDs) is highly conserved, their transmembrane domains (TMDs) forming the translocation pathway exhibit distinct folds and topologies, suggesting that during evolution the ancient motor domains were combined with different transmembrane mechanical systems to orchestrate a variety of cellular processes. In recent years, it has become increasingly evident that the distinct TMD folds are best suited to categorize the multitude of ABC transporters. We therefore propose a new ABC transporter classification that is based on structural homology in the TMDs.

KW - ABC transporters

KW - ATPases

KW - X-ray crystallography

KW - cryo-EM

KW - membrane proteins

KW - molecular machines

KW - phylogeny

KW - primary active transporters

KW - sequence alignment

KW - structural biology

U2 - 10.1002/1873-3468.13935

DO - 10.1002/1873-3468.13935

M3 - Article

C2 - 32978974

SN - 0014-5793

VL - 594

SP - 3767

EP - 3775

JO - FEBS Letters

JF - FEBS Letters

IS - 23

M1 - 1873-3468.13935

ER -

Structural and functional diversity calls for a new classification of ABC transporters

Samenvatting

Toegang tot document

Handle.net

Vingerafdruk

Citeer dit