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TitleCryo-EM structures of the human NaS1 and NaDC1 transporters revealed the elevator transport and allosteric regulation mechanism.
Journal, issue, pagesSci Adv, Vol. 10, Issue 13, Page eadl3685, Year 2024
Publish dateMar 29, 2024
AuthorsXimin Chi / Yiming Chen / Yaning Li / Lu Dai / Yuanyuan Zhang / Yaping Shen / Yun Chen / Tianhao Shi / Haonan Yang / Zilong Wang / Renhong Yan /
PubMed AbstractThe solute carrier 13 (SLC13) family comprises electrogenic sodium ion-coupled anion cotransporters, segregating into sodium ion-sulfate cotransporters (NaSs) and sodium ion-di- and-tricarboxylate ...The solute carrier 13 (SLC13) family comprises electrogenic sodium ion-coupled anion cotransporters, segregating into sodium ion-sulfate cotransporters (NaSs) and sodium ion-di- and-tricarboxylate cotransporters (NaDCs). NaS1 and NaDC1 regulate sulfate homeostasis and oxidative metabolism, respectively. NaS1 deficiency affects murine growth and fertility, while NaDC1 affects urinary citrate and calcium nephrolithiasis. Despite their importance, the mechanisms of substrate recognition and transport remain insufficiently characterized. In this study, we determined the cryo-electron microscopy structures of human NaS1, capturing inward-facing and combined inward-facing/outward-facing conformations within a dimer both in apo and sulfate-bound states. In addition, we elucidated NaDC1's outward-facing conformation, encompassing apo, citrate-bound, and -(-amylcinnamoyl) anthranilic acid (ACA) inhibitor-bound states. Structural scrutiny illuminates a detailed elevator mechanism driving conformational changes. Notably, the ACA inhibitor unexpectedly binds primarily anchored by transmembrane 2 (TM2), Loop 10, TM11, and TM6a proximate to the cytosolic membrane. Our findings provide crucial insights into SLC13 transport mechanisms, paving the way for future drug design.
External linksSci Adv / PubMed:38552027 / PubMed Central
MethodsEM (single particle)
Resolution2.5 - 3.3 Å
Structure data

37320

8w6c

EMDB-37320, PDB-8w6c:
CryoEM structure of NaDC1 with Citrate
Method: EM (single particle) / Resolution: 2.7 Å

37321

8w6d

EMDB-37321, PDB-8w6d:
CryoEM structure of NaDC1 in apo state
Method: EM (single particle) / Resolution: 2.5 Å

37322

8w6g

EMDB-37322, PDB-8w6g:
NaDC1 with inhibitor ACA
Method: EM (single particle) / Resolution: 3.3 Å

37323

8w6h

EMDB-37323, PDB-8w6h:
NaS1 with sulfate - IN/IN state
Method: EM (single particle) / Resolution: 3.1 Å

37329

8w6n

EMDB-37329, PDB-8w6n:
NaS1 with sulfate in IN/OUT state
Method: EM (single particle) / Resolution: 3.2 Å

37330

8w6o

EMDB-37330, PDB-8w6o:
NaS1 in IN/IN state
Method: EM (single particle) / Resolution: 2.9 Å

37332

8w6t

EMDB-37332, PDB-8w6t:
NaS1 in IN/OUT state
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-CIT:
CITRIC ACID

ChemComp-3PH:
1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE

ChemComp-HOH:
WATER


ChemComp, No image

ChemComp-VIJ:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-CLR:
CHOLESTEROL

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / Citrate / transporter / NaDC1 / inhibitor / sulfate / NaS1 / apo state / IN/IN state / IN/OUT state

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