7QKS
Cryo-EM structure of ABC transporter STE6-2p from Pichia pastoris in apo conformation at 3.1 A resolution
Summary for 7QKS
| Entry DOI | 10.2210/pdb7qks/pdb |
| Related | 7QKR |
| EMDB information | 14050 |
| Descriptor | Plasma membrane ATP-binding cassette transporter required for the export of a-factor, (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en (2 entities in total) |
| Functional Keywords | abc transporter, abcb, mdr, membrane protein, pichia pastoris, transport protein |
| Biological source | Komagataella phaffii CBS 7435 |
| Total number of polymer chains | 1 |
| Total formula weight | 145519.07 |
| Authors | Schleker, E.S.M.,Reinhart, C. (deposition date: 2021-12-18, release date: 2022-10-26, Last modification date: 2024-07-17) |
| Primary citation | Schleker, E.S.M.,Buschmann, S.,Xie, H.,Welsch, S.,Michel, H.,Reinhart, C. Structural and functional investigation of ABC transporter STE6-2p from Pichia pastoris reveals unexpected interaction with sterol molecules. Proc.Natl.Acad.Sci.USA, 119:e2202822119-e2202822119, 2022 Cited by PubMed Abstract: Adenosine triphosphate (ATP)-binding cassette (ABC) transporters are multidomain transmembrane proteins, which facilitate the transport of various substances across cell membranes using energy derived from ATP hydrolysis. They are important drug targets since they mediate decreased drug susceptibility during pharmacological treatments. For the methylotrophic yeast , a model organism that is a widely used host for protein expression, the role and function of its ABC transporters is unexplored. In this work, we investigated the ABC-B transporter STE6-2p. Functional investigations revealed that STE6-2p is capable of transporting rhodamines in vivo and is active in the presence of verapamil and triazoles in vitro. A phylogenetic analysis displays homology among multidrug resistance (MDR) transporters from pathogenic fungi to human ABC-B transporters. Further, we present high-resolution single-particle electron cryomicroscopy structures of an ABC transporter from in the apo conformation (3.1 Å) and in complex with verapamil and adenylyl imidodiphosphate (AMP-PNP) (3.2 Å). An unknown density between transmembrane helices 4, 5, and 6 in both structures suggests the presence of a sterol-binding site of unknown function. PubMed: 36256814DOI: 10.1073/pnas.2202822119 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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