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TitleStructural and functional investigation of ABC transporter STE6-2p from reveals unexpected interaction with sterol molecules.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 119, Issue 43, Page e2202822119, Year 2022
Publish dateOct 25, 2022
AuthorsE Sabine M Schleker / Sabine Buschmann / Hao Xie / Sonja Welsch / Hartmut Michel / Christoph Reinhart /
PubMed AbstractAdenosine triphosphate (ATP)-binding cassette (ABC) transporters are multidomain transmembrane proteins, which facilitate the transport of various substances across cell membranes using energy ...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.
External linksProc Natl Acad Sci U S A / PubMed:36256814 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 3.2 Å
Structure data

14049

7qkr

EMDB-14049: Cryo-EM structure of ABC transporter STE6-2p from Pichia pastoris in apo conformation at 3.1 A resolution
PDB-7qkr: Cryo-EM structure of ABC transporter STE6-2p from Pichia pastoris with Verapamil at 3.2 A resolution
Method: EM (single particle) / Resolution: 3.2 Å

14050

7qks

EMDB-14050, PDB-7qks:
Cryo-EM structure of ABC transporter STE6-2p from Pichia pastoris in apo conformation at 3.1 A resolution
Method: EM (single particle) / Resolution: 3.1 Å

Chemicals

ChemComp-I6H:
Dexverapamil / medication, channel blocker*YM

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-9Z9:
(3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en / detergent*YM

Source
  • komagataella phaffii cbs 7435 (fungus)
KeywordsTRANSPORT PROTEIN / ABC transporter / ABCB / MDR / membrane protein / Pichia pastoris

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