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

Author

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

Published
2020
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9. Characterization of the Lactococcus lactis pepNgene encoding an aminopeptidase homologous to mammalian aminopeptidase N

Author

Tan, Paris S.T., van Alen-Boerrigter, Ingrid J., Poolman, Bert, Siezen, Roland J., de Vos, Willem M., and Konings, W.N.

Abstract

The nucleotide sequence of the pepNgene from Lactococcus lactisencoding a zinc-metallo aminopeptidase has been determined. The open reading frame of 2,538 base pairs encodes a protein with a calculated Mrof 95,368, which agrees with the apparent Mrof 95,000 of the gene product which was identified by polyclonal antibodies raised against the purified aminopeptidase. The amino acid sequence of the aminopeptidase of L. lactiswas found to be similar to the corresponding enzymes of human, rat and mouse, with almost 30% of the residues identical. Also, a highly conserved area was identified which has similarity with the active site of thermolysin. A zinc-binding site, as well as the catalytic site for PepN, is predicted to lie within this conserved stretch. Putative promoter regions upstream of PepN were confirmed by primer extension analysis.

Published
1992
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10. Structural and functional diversity calls for a new classification of ABC transporters

Author

Oded Lewinson, D. Peter Tieleman, Balázs Sarkadi, Xin Gong, Elisabeth P. Carpenter, Nieng Yan, Daniel Kahne, Po-Chao Wen, Christopher M. Koth, Rachelle Gaudet, Elie Dassa, Daniel M. Rosenbaum, Show Ling Shyng, Youngsook Lee, Vassilis Koronakis, Konstantinos Beis, Yigong Shi, Damian C. Ekiert, Kazumitsu Ueda, I. Barry Holland, Roland Lill, Satoshi Murakami, Dirk Jan Slotboom, Lei Chen, Stephen G. Aller, Franck Duong Van Hoa, Michael Dean, Peng Zhang, Lutz Schmitt, Enrico Martinoia, Geoffrey Chang, Bert Poolman, Emad Tajkhorshid, András Váradi, Erwin Schneider, Jochen Zimmer, Heather W. Pinkett, Hongjin Zheng, Yihua Huang, Christoph Thomas, Hiroaki Kato, Robert Ford, Robert Tampé, Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Enzymology, Thomas, Christoph [0000-0001-7441-1089], Aller, Stephen G [0000-0003-0379-5534], Beis, Konstantinos [0000-0001-5727-4721], Dean, Michael [0000-0003-2234-0631], Lill, Roland [0000-0002-8345-6518], Murakami, Satoshi [0000-0001-5553-7663], Pinkett, Heather W [0000-0002-1102-1515], Poolman, Bert [0000-0002-1455-531X], Schmitt, Lutz [0000-0002-1167-9819], Slotboom, Dirk J [0000-0002-5804-9689], Tieleman, D Peter [0000-0001-5507-0688], Ueda, Kazumitsu [0000-0003-2980-6078], Váradi, András [0000-0002-2722-7120], Wen, Po-Chao [0000-0002-6049-6904], Tampé, Robert [0000-0002-0403-2160], and Apollo - University of Cambridge Repository

Subjects
Protein Folding, [SDV]Life Sciences [q-bio], Biophysics, ATPases, Sequence alignment, ATP-binding cassette transporter, membrane proteins, Computational biology, Biology, phylogeny, Biochemistry, Article, 03 medical and health sciences, Protein Domains, Phylogenetics, ddc:570, molecular machines, Genetics, structural biology, Molecular Biology, 030304 developmental biology, X-ray crystallography, 0303 health sciences, 030302 biochemistry & molecular biology, ABC Transporters, Transporter, Cell Biology, primary active transporters, Molecular machine, Transmembrane protein, Transmembrane domain, Structural biology, sequence alignment, ddc:540, cryo-EM, ATP-Binding Cassette 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 currently comprises seven different types based on structural homology in the TMDs.

Published
2020

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