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TitleTransport mechanism of human bilirubin transporter ABCC2 tuned by the inter-module regulatory domain.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 1061, Year 2024
Publish dateFeb 5, 2024
AuthorsYao-Xu Mao / Zhi-Peng Chen / Liang Wang / Jie Wang / Cong-Zhao Zhou / Wen-Tao Hou / Yuxing Chen /
PubMed AbstractBilirubin is mainly generated from the breakdown of heme when red blood cells reach the end of their lifespan. Accumulation of bilirubin in human body usually leads to various disorders, including ...Bilirubin is mainly generated from the breakdown of heme when red blood cells reach the end of their lifespan. Accumulation of bilirubin in human body usually leads to various disorders, including jaundice and liver disease. Bilirubin is conjugated in hepatocytes and excreted to bile duct via the ATP-binding cassette transporter ABCC2, dysfunction of which would lead to Dubin-Johnson syndrome. Here we determine the structures of ABCC2 in the apo, substrate-bound and ATP/ADP-bound forms using the cryo-electron microscopy, exhibiting a full transporter with a regulatory (R) domain inserted between the two half modules. Combined with substrate-stimulated ATPase and transport activity assays, structural analysis enables us to figure out transport cycle of ABCC2 with the R domain adopting various conformations. At the rest state, the R domain binding to the translocation cavity functions as an affinity filter that allows the substrates of high affinity to be transported in priority. Upon substrate binding, the R domain is expelled from the cavity and docks to the lateral of transmembrane domain following ATP hydrolysis. Our findings provide structural insights into a transport mechanism of ABC transporters finely tuned by the R domain.
External linksNat Commun / PubMed:38316776 / PubMed Central
MethodsEM (single particle)
Resolution3.32 - 4.17 Å
Structure data

36691

8jx7

EMDB-36691, PDB-8jx7:
Cryo-EM structure of human ABC transporter ABCC2
Method: EM (single particle) / Resolution: 3.6 Å

36709

8jxq

EMDB-36709, PDB-8jxq:
Cryo-EM structure of bilirubin ditaurate (BDT) bound human ABC transporter ABCC2
Method: EM (single particle) / Resolution: 3.32 Å

36713

8jxu

EMDB-36713, PDB-8jxu:
Cryo-EM structure of human ABC transporter ABCC2 under active turnover condition
Method: EM (single particle) / Resolution: 3.55 Å

36719

8jy4

EMDB-36719, PDB-8jy4:
Cryo-EM structure of human ABC transporter ABCC2 in apo' state
Method: EM (single particle) / Resolution: 3.58 Å

36720

8jy5

EMDB-36720, PDB-8jy5:
Cryo-EM structure of human ABC transporter ABCC2 in apo" state
Method: EM (single particle) / Resolution: 4.17 Å

Chemicals

ChemComp-CLR:
CHOLESTEROL

ChemComp-FEI:
2-[3-[5-[(E)-(4-ethenyl-3-methyl-5-oxidanylidene-pyrrol-2-ylidene)methyl]-2-[[5-[(3-ethenyl-4-methyl-5-oxidanylidene-pyrrol-2-ylidene)methyl]-4-methyl-3-[3-oxidanylidene-3-(2-sulfoethylamino)propyl]-1H-pyrrol-2-yl]methyl]-4-methyl-1H-pyrrol-3-yl]propanoylamino]ethanesulfonic acid

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / ATP-dependent transporter / conjugated organic anions transporter / ATP hydrolyzes / bilirubin / ABC transporter

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