7qks | pdb_00007qks

Cryo-EM structure of ABC transporter STE6-2p from Pichia pastoris in apo conformation at 3.1 A resolution

spinqualitylabelsall models 7qks, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7qks is a 1 chain structure with sequence from Komagataella phaffii CBS 7435. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.1Å Ligands: 9Z9 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function F2QQK6_KOMPC Publication Abstract from PubMed 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 Pichia pastoris, 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 Pichia 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 P. pastoris in the apo conformation (3.1 A) and in complex with verapamil and adenylyl imidodiphosphate (AMP-PNP) (3.2 A). An unknown density between transmembrane helices 4, 5, and 6 in both structures suggests the presence of a sterol-binding site of unknown function. Structural and functional investigation of ABC transporter STE6-2p from Pichia pastoris reveals unexpected interaction with sterol molecules.,Schleker ESM, Buschmann S, Xie H, Welsch S, Michel H, Reinhart C Proc Natl Acad Sci U S A. 2022 Oct 25;119(43):e2202822119. doi: , 10.1073/pnas.2202822119. Epub 2022 Oct 18. PMID:36256814 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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