ABCG: a new fold of ABC exporters and a whole new bag of riddles!
| Autor: | Jorgaq Pata, Atanu Banerjee, Alexis Moreno, Pierre Falson, Rajendra Prasad |
|---|---|
| Přispěvatelé: | Amity University, Institut de biologie et chimie des protéines [Lyon] (IBCP), Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon, Rossen Donev, Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 2021 |
| Předmět: |
0303 health sciences
Subfamily [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] Abcg2 biology Chemistry ABCG family Transporter ATP-binding cassette transporter Biological membrane PDR subfamily Translocon 03 medical and health sciences Transmembrane domain 0302 clinical medicine Biochemistry Transmembrane domains biology.protein ABC transporter Efflux Nucleotide-binding domains 030217 neurology & neurosurgery Non-catalytic NBS 030304 developmental biology |
| Zdroj: | Advances in Protein Chemistry and Structural Biology ISBN: 9780128220870 Advances in Protein Chemistry and Structural Biology Rossen Donev. Advances in Protein Chemistry and Structural Biology, 123, Elsevier, pp.163-191, 2021, ⟨10.1016/bs.apcsb.2020.09.006⟩ |
| Popis: | International audience; ATP-binding cassette (ABC) superfamily comprises membrane transporters that power the active transport of substrates across biological membranes. These proteins harness the energy of nucleotide binding and hydrolysis to fuel substrate translocation via an alternating-access mechanism. The primary structural blueprint is relatively conserved in all ABC transporters. A transport-competent ABC transporter is essentially made up of two nucleotide-binding domains (NBDs) and two transmembrane domains (TMDs). While the NBDs are conserved in their primary sequence and form at their interface two nucleotide-binding sites (NBSs) for ATP binding and hydrolysis, the TMDs are variable among different families and form the translocation channel. Transporters catalyzing the efflux of substrates from the cells are called exporters. In humans, they range from A to G subfamilies, with the B, C and G subfamilies being involved in chemoresistance. The recently elucidated structures of ABCG5/G8 followed by those of ABCG2 highlighted a novel structural fold that triggered extensive research. Notably, suppressor genetics in the orthologous yeast Pleiotropic Drug Resistance (PDR) subfamily proteins have pointed to a crosstalk between TMDs and NBDs modulating substrate export. Considering the structural information provided by their neighbors from the G subfamily, these studies provide mechanistic keys and posit a functional role for the non-hydrolytic NBS found in several ABC exporters. The present chapter provides an overview of structural and functional aspects of ABCG proteins with a special emphasis on the yeast PDR systems. |
| Databáze: | OpenAIRE |
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