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TitlePlacing steroid hormones within the human ABCC3 transporter reveals a compatible amphiphilic substrate-binding pocket.
Journal, issue, pagesEMBO J, Vol. 42, Issue 17, Page e113415, Year 2023
Publish dateSep 4, 2023
AuthorsJie Wang / Xu Li / Fang-Fang Wang / Meng-Ting Cheng / Yao-Xu Mao / Shu-Cheng Fang / Liang Wang / Cong-Zhao Zhou / Wen-Tao Hou / Yuxing Chen /
PubMed AbstractThe human ABC transporter ABCC3 (also known as MRP3) transports a wide spectrum of substrates, including endogenous metabolites and exogenous drugs. Accordingly, it participates in multiple ...The human ABC transporter ABCC3 (also known as MRP3) transports a wide spectrum of substrates, including endogenous metabolites and exogenous drugs. Accordingly, it participates in multiple physiological processes and is involved in diverse human diseases such as intrahepatic cholestasis of pregnancy, which is caused by the intracellular accumulation of bile acids and estrogens. Here, we report three cryogenic electron microscopy structures of ABCC3: in the apo-form and in complexed forms bound to either the conjugated sex hormones β-estradiol 17-(β-D-glucuronide) and dehydroepiandrosterone sulfate. For both hormones, the steroid nuclei that superimpose against each other occupy the hydrophobic center of the transport cavity, whereas the two conjugation groups are separated and fixed by the hydrophilic patches in two transmembrane domains. Structural analysis combined with site-directed mutagenesis and ATPase activity assays revealed that ABCC3 possesses an amphiphilic substrate-binding pocket able to hold either conjugated hormone in an asymmetric pattern. These data build on consensus features of the substrate-binding pocket of MRPs and provide a structural platform for the rational design of inhibitors.
External linksEMBO J / PubMed:37485728 / PubMed Central
MethodsEM (single particle)
Resolution3.07 - 3.65 Å
Structure data

35043

8hvh

EMDB-35043, PDB-8hvh:
Cryo-EM structure of ABC transporter ABCC3
Method: EM (single particle) / Resolution: 3.07 Å

35049

8hw2

EMDB-35049, PDB-8hw2:
Cryo-EM structure of beta-estradiol 17-(beta-D-glucuronide)-bound human ABC transporter ABCC3 in nanodiscs
Method: EM (single particle) / Resolution: 3.65 Å

35050

8hw4

EMDB-35050, PDB-8hw4:
Cryo-EM structure of dehydroepiandrosterone sulfate-bound human ABC transporter ABCC3 in nanodiscs
Method: EM (single particle) / Resolution: 3.52 Å

Chemicals

ChemComp-U38:
Estradiol-17beta-glucuronide

ChemComp-ZWY:
17-oxoandrost-5-en-3beta-yl hydrogen sulfate

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / ABC transporter / TRANSPORT PROTEIN / multidrug resistance protein

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